Curriculum Vitae List of Publications and Research Funding ...

Curriculum Vitae List of Publications

and Research Funding

Shahriar Mobashery Address: Department of Chemistry and Biochemistry 251 Nieuwland Science Center University of Notre Dame Notre Dame, IN 46556 USA Telephone: (574) 631-2933 FAX: (574) 631-6652 e-mail: [email protected] Date of Birth: May 17, 1958 Education: University of Southern California, Los Angeles, California B.S. Biological Sciences, 1980 B.S. Chemistry, 1981 University of Chicago, Chicago, Illinois Ph.D. Chemistry, 1985 Experience: Predoctoral Research; University of Southern California, Department of Chemical Engineering,

Professor T.F. Yen's laboratory, 1979-1981. University of Chicago, Department of Chemistry, Professor Michael Johnston's laboratory, 1981-

1985. Postdoctoral Research; Rockefeller University, Laboratory of Bioorganic Chemistry and

Biochemistry, the late Professor Emil Thomas Kaiser's laboratory, 1986-1988. Assistant Professor; Department of Chemistry, Wayne State University, 1989-1994. Associate Professor; Department of Chemistry, Wayne State University, 1994-1997. Professor; Department of Chemistry, Wayne State University, 1997-2003. Professor; Departments of Pharmacology and Biochemistry and Molecular Biology, Wayne State

University, 2000-2003. Chair; Division of Biochemistry of the Department of Chemistry, 1996-2000. Director, Institute for Drug Design, 2000-2003. Navari Family Professor in Life Sciences; Department of Chemistry and Biochemistry; University

of Notre Dame, 2003-present.

Shahriar Mobashery Curriculum Vitae

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Membership in Professional Societies: American Chemical Society American Association for Advancement of Science American Society for Microbiology Sigma Xi American Society for Biochemistry and Molecular Biology New York Academy of Sciences Honors and Awards: The Outstanding Senior Recognition Award, University of Southern California, 1980 and 1981 Sigma Xi Award, University of Southern California, 1981 The Rockefeller Postdoctoral Fellowship, 1986-1987 The National Institutes of Health Postdoctoral Fellowship, 1987-1988 The Jane Coffin Child Postdoctoral Fellowship, 1987 (declined) Award of the Lectureship of the Society of Synthetic Organic Chemistry (Japan), 1995 Career Development Chair Award, WSU, 1996 Award of Excellence in Teaching, 1997. Charles H. Gershenson Distinguished Faculty Fellow, 1999-2001 Honorary Charter Member of the Argentinian Society for Organic Chemistry, 2003-present. Fellow of the American Academy for the Advancement of Science (AAAS), elected 2007. Astellas USA Foundation Award of the American Chemical Society, 2007. Research Achievement Award, University of Notre Dame, 2012. Fellow, Science Without Borders, Brazil, 2014-2016 Professional Activities: Consultant, Salk Institute Biotechnology/Industrial Associates (SIBIA), 1989-1992, Affymax

Corp., 1996-1998, Procter & Gamble Pharmaceuticals, 1997-1998, Aurora Biosciences Corp., 1998-1999, Guilford Pharmaceutical Co., 2000-2002, NewBiotics, Inc., 2000-2003, Rigel, Inc., 2003-2004. Cubist Pharmaceutical Co., 2012. Consultant to law firms 1993-present.

Editorial Board Member of Pharmaceutical and Medicinal Chemistry, 1995-2014, J. Antibiot., 1998-2006 and 2012-present, Letters in Drug Design and Discovery, 2002-2010; Open Organic Chemistry Journal, 2006-2010. Antimicrob. Agents Chemother., 1999-2013. Cancer Management and Research, 2008-2015. Microbial Drug Resistance, 2009-2017. Bioorganic Chemistry, 2000-present; Current Organic Synthesis, 2002-present, Lett. Org. Chem., 2002-present; Mini Reviews in Organic Chemistry, 2002-present. Chemical Biology & Drug Design, 2006-present. J. Biol. Chem., 2012-2017. ACS Infectious Diseases, 2014-present.

Scientific Advisory Board, NewBiotics, Inc. 2000-2003. Panel Member, NIH Summit on Development of Infectious Diseases Therapeutics, September

2000. Panel Member, NIH Summit on Development of Infectious Diseases Therapeutics, August 2004. Section Co-Editor, Current Opinion in Chemical Biology, 2003. American Cancer Society, Advisory Committee on Biochemistry and Endocrinology (Study

Section), 1994-1996, 1999-2000. Member, NIH Bioorganic and Natural Products (BNP) Study Section (became the SBC-B Study

Section), 2001-2005. Ad hoc reviewer for the National Science Foundation, National Institutes of Health, Department of Veterans Affairs, American Chemical Society (Petroleum Research Fund), French Ministry of Research, Swiss National Science Foundation, Israeli Science


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Foundation, Minnesota Sea Grant Program, Medical Research Council of the United Kingdom, Biotechnology and Biological Sciences Research Council (of the UK), Engineering Research Council of Canada, Health Research Board of Ireland, Netherlands Organisation for Scientific Research (NWO), Natural Sciences and Engineering Research Council of Canada (NSERC), Research Grants Council (RGC) of Hong Kong, Health Research Borad of Ireland, US-Israel Binational Science Foundation, National Science Foundation of Belgium, Japan Society for the Promotion of Science (JSPS), Portuguese Foundation for Science and Technology (FCT), Agency for Science, Technology and Research (A*STAR) Biomedical Research Council (BMRC) of Singapore, U.S.-Israel Binational Science Foundation, French Research Agency (ANR), The Welcome Trust, The MacArthur Foundation, Canadian Institutes of Health Research (CIHR), Indiana CTSI, French National Research Agency (ANR), The Sir Henry Wellcome Postdoctoral Fellowships, National Science Centre of Poland, South African Medical Research Council. Member, Site Visit Team for the National Cancer Institute, May 1995. Ad hoc reviewer for the following journals (1989-present): J. Am. Chem. Soc., Proc. Nat. Acad. Sci. U.S.A., Biochemistry, Chemistry & Biology,Tetrahedron, Tetrahedron Lett., Bioorg. Med. Chem., Bioorg. Med. Chem . Lett., J. Med. Chem., J. Biol. Chem., J. Biomol. Struc. Dynam., J. Org. Chem., Proteins: Structure, Function, and Genetics, Pharm. Med. Chem., J. Chem. Soc. Chem. Comm., Antimicrob. Agents Chemother, Bioorganic Chemistry, Arch. Biochem. Biophys, Protein Engineering, Molecular Medicine Today, Organic Prep. Proc. Int., Eur. J. Biochem., African J. Biotech., Archives of Biochemistry and BiophysicsJ. Bacteriol., Protein Science, Brit. J. Cancer, J. Mol. Biol., Medical Principles and Practice, J. Mol. Biol., Biochem. Biophys. Acta, Org. Lett., Microbiology, J. Phys. Chem., Inorgan. Chem., Molec. Micro., ChemBioChem. , Structure, Biochimica et Biophysica Acta, FEMS Micro. Lett., Org. Biomolec. Chem., International Union of Biochemistry and Molecular Biology Life, Biomacromolecules, Langmuir, ACS Chem. Biol., BBA - Proteins and Proteomics, Eur. J. Org. Chem., Nature Reviews Drug Discovery, Natue Nanotechnology, Chemical Biology & Drug Design, Trends in Microbiology, ACS Journal of Combinatorial Chemistry, Int. J. Cancer, Eur. J. Med. Chem., J. Infection, Perspect. Med. Chem., Applied and Environmental Microbiology, Angewandte Chemie, Lett. Drug Design and Discovery, ChemMedChem, Synthesis, PLoS One, Biophysical J., J. Royal Soc. Interface, Acc. Chem. Res., Expt. Rev. Anti-infec. Ther., J. Pharm. Pharmacol., Future Med. Chem., International J. Mol. Sci.; Cancer Biol & Therapy; Xomputers in Biology, Chem. Rev. and Medicine; Prot. & Pept. Lett., Med. Chem. Comm., Chemical Science; Org. & Biomol. Chem.; Chemotherapy; Med. Chem. Comm.; Annu. Rev. of Biochem.; Int. J. Med. Chem.; Computers Biol. Medicine; Scientific Reports; Molecules; ACS Applied Materials & Interfaces, Scientific Reports, Appl. Biochem and Biotech., J. Chem. Theory & Comp., Global Policy; Phosphorus, Sulfur, and Silicon and the Related Elements; Philosophical Transactions B; Microbiol. Open; Chemical Record; J. Biol. Phys.; Drug Design, Development and Therapy; Scientific Reports; J. Braz. Chem. Soc.; Cell Chem. Biol.; Protein & Peptide Lett.; Springer Plus; Cell Chemical Biology; Microbial Cell Factories; Molecules; eLife; Expt. Rev. Clinic. Parmacol.; J. Enz. Inh. Med. Chem.; J. Infec. Pub. Health; Genome Biol. Evolu.; Braz. J. Phram. Sci.; Sci. Report; Nat. Chem.; Cell Chem. Biol.; J. Infect.


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Pub. Health; ACS Applied Materials & Interfaces; SAR and QSAR in Environmental Research; Curr. Op. Drug Metabol.; Microb. Pathogenesis; EMBO J.; J. Molecular Graphics and Modelling; J. Infect. Pub. Health; Virulence and J. Antibiot. Chairman, The Enzyme Mechanisms Section of the XII Midwest Enzyme Chemistry Conference,

October 1992, Chicago, Illinois Chairman, The Enzyme Mechanisms Section of the Second International Symposium on

Bioorganic Chemistry, Fukuoka, Japan, June 1993 Organizer and Chairman, Symposium on "Rational Drug Design and Enzyme Mechanisms", The

joint 26th Central Regional/27th Great Lakes Regional ACS meeting, Ann Arbor, Michigan, June1-3, 1994

Organizer and Chairman, Symposium on "Recent Developments in Antibacterials and Mechanisms of Resistance", The Central ACS meeting, Midland, Michigan, May 1997

Organizer, Symposium on "Recent Developments in Antibacterials and Mechanisms of Resistance", Wayne State University, May 1997

Organizer, XVIII Midwest Enzyme Chemistry Conference, Evanston, Illinois, October 1998. Organizer, Symposium on β-Lactamases, the National Meeting of the American Society for

Microbiology, Orlando, Illinois, Florida, 2001. Who’s Who in America, 2002-present. Who’s Who in the World, 2002-present. Who’s Who in Science and Engineering, 2003-present. Who’s Who in Sciences Higher Education (WWSHE), 2004-present. Organizing Committee Member, Meeting of the International Union of Biochemistry and

Molecular Biology (IUBMB), Toronto, Canada, 2003. Advisory Board Member of the Department of Defense Center of Excellence in Breast Cancer at

Wayne State University, 2002-2003. Co-Editor (with John Richards) for the issue of Curr. Opin. Chem. Biol. on Complex Biological

Systems (2003). Co-Editor (with Steve Brickner) for the issue of Curr. Opin. Microbiol. on Antibiotics (2007). Co-Editor (with Didier Mazel) for the Curr. Opin. Microbiol., Antimicrobials Section (2012). Organizer, Conference entitled “Novel Antibiotics, Old and New Targets”, June 2008. Advisory Board Member, Faculty of 1000 Biology, 2008-2010. Member, NIH Drug Discovery and Mechanisms of Antimicrobial Resistance Study Section

(DDR), 2009-2012. Organizer, Symposium entitled “Early Events in Cell Wall Recycling”, the 110th American

Society for Microbiology General Meeting, San Diego, California, 2010. Co-founder (with Mayland Chang) of Nupromed, LLC, 2009-present. Co-Chair (with Jared Silverman), Gordon Research Conference on New Antibacterial Discovery

& Development, 2014. Scientific and Clinical Advisory Board, Valevia Pharmaceuticals, Binningen, Switzerland; 2010-

2012. Board of Directors, Cancer Drug Delivery Research Foundation, 2012-present. Member, Board of Professors, University of Siena, Italy, 2013-present. Publications: Citations: >17,500; H-index 63; i10-index 256


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1. Mobashery, S.; Johnston, M. A New Approach to the Preparation of N-Carboxy-α-Amino Acid Anhydrides, J. Org. Chem. 1985, 50, 2200.

2. Mobashery, S.; Lerner, S. A.; Johnston, M. Conscripting β-Lactamase for Use in Drug

Delivery. Synthesis and Biological Activity of a Cephalosporin C10-Ester of an Antibiotic Dipeptide, J. Am. Chem. Soc. 1986, 108, 1685.

3. Mobashery, S.; Johnston, M. Reactions of Escherichia coli TEM β-Lactamase with

Cephalothin and with C10-Dipeptidyl Cephalosporin Esters, J. Biol. Chem. 1986, 261, 7879.

4. Mobashery, S.; Johnston, M. A Novel Approach to Deacylation of Ceph-3-em Esters,

Tetrahedron Lett. 1986, 27, 3333. 5. Mobashery, S.; Johnston, M. Preparation of Ceph-3-em Esters Unaccompanied by Δ3 → Δ2

Isomerization of the Cephalosporin, J. Org. Chem. 1986, 51, 4723. 6. Mobashery, S.; Johnston, M. Inactivation of Alanine Racemase by β-Chloro-L-Alanine

Released Enzymatically from Amino Acid and Peptidyl C10-Esters of Deacetylcephalothin, Biochemistry 1987, 26, 5878.

7. Mobashery, S.; Lerner, S.; Johnston, M. Monitoring β-Lactamase Activity In Vivo by 13C

Nuclear Magnetic Resonance Spectroscopy, Antimicrob. Agents Chemother. 1988, 32, 1196.

8. Mobashery, S.; Kaiser, E. T. Identification of Active Site Amino Acid Residues in the

Catalytic Subunit of Bovine Cyclic AMP-Dependent Protein Kinase by Peptide-Based Affinity Inactivators, Biochemistry 1988, 27, 3691.

9. Radziejewski, C.; Miller, W. T.; Mobashery, S.; Goldberg, A.; Kaiser, E. T. Purification of

Recombinant v-src Gene-Product from Saccharomyces Servisiae and Analysis of Peptidic Substrates to the Enzyme, Biochemistry 1989, 28, 9047.

10. Mobashery, S.; Ghosh, S.; Tamura, S. Y.; Kaiser, E. T. Design of an Effective Mechanism-

Based Inactivator for a Zinc Protease, Proc. Natl. Acad. Sci. U. S. A. 1990, 87, 578. 11. Mobashery, S.; Doughty, M.; Kaiser, E. T. Inactivation of the Catalytic Subunit of Bovine

Cyclic AMP-Dependent Protein Kinase by a Peptide-Based Affinity Inactivator, Biopolymers 1990, 29, 131.

12. Ghosh, S. S.; Wu, Y. Q.; Mobashery, S. Peptidic Mechanism-Based Inactivators for

Carboxypeptidase A, J. Biol. Chem. 1991, 266, 8759. 13. Wu, Y. Q.; Mobashery, S. Targeting Renal Dipeptidase (Dehydropeptidase I) for

Inactivation by Mechanism-Based Inactivators, J. Med. Chem. 1991, 34, 1914. 14. Goren, Z.; Heeg, M. J.; Mobashery, S. Facile Chloride Substitution of Activated Alcohols

by Triphosgene: Application to Cephalosporin Chemistry, J. Org. Chem. 1991, 54, 7186. 15. Wilder, R.; Mobashery, S. The Use of Triphosgene in Preparation of N-Carboxy-α-Amino

Acid Anhydrides, J. Org. Chem. 1992, 57, 2755.


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16. Zafaralla, G.; Mobashery, S. Facilitation of the Δ2 → Δ1 Pyrroline Tautomerization of Carbapenem Antibiotics by the Highly Conserved Arginine-244 of Class A β-Lactamases During the Course of Turnover, J. Am. Chem. Soc. 1992, 114, 1505.

17. Zafaralla, G.; Manavathu, E. K.; Lerner, S. A.; Mobashery; S. Elucidation of the Role of

Arg-244 in the Turnover Processes of Class A β-Lactamases, Biochemistry 1992, 31, 3847.

18. Ghosh, S. S.; Said-Nejad, O.; Roestamadji, J.; Mobashery, S. The First Mechanism-Based

Inactivator for Angiotensin-Converting Enzyme, J. Med. Chem. 1992, 35, 4175. 19. Imtiaz, U; Billings, E.; Knox, J. R.; Manavathu, E. K., Lerner, S. A.; Mobashery, S.

Inactivation of Class A β-Lactamases by Clavulanic Acid: The Role of Arginine-244 in a Proposed Nonconcerted Sequence of Events, J. Am. Chem. Soc. 1993, 115, 4435.

20. Zafaralla, G.; Mobashery, S. Evidence for a New Enzyme-Catalyzed Reaction Other Than

β-Lactam Hydrolysis in Turnover of a Penem by the TEM-1 β-Lactamase, J. Am. Chem. Soc. 1993, 115, 4962.

21. Levy, O. E.; Taibi, P.; Mobashery, S.; Ghosh, S. S. A Mechanism-Based Inactivation Study

of Neutral Endopeptidase 24.11, J. Med. Chem. 1993, 36, 2408. 22. Imtiaz, U.; Manavathu, E. K.; Lerner, S. A.; Mobashery; S. A Critical Hydrogen Bond by

Ser-235 for the Cephalosporinase Activity of the TEM-1 β-Lactamase, Antimicrob. Agents Chemother. 1993, 37, 2438.

23. Siregar, J. J.; Lerner, S. A.; Mobashery, S. Purification and Characterization of

Aminoglycoside 3'-Phosphotransferase Type II, and Kinetic Comparison with a New Mutant Enzyme, Antimicrob. Agents Chemother. 1994, 38, 641.

24. Grapsas, I.; Cho, Y. J.; Mobashery, S. N-(t-Butoxycarbonyloxy)-5-norbornene-endo-2,3-

dicarboximide, A Reagent for the Regioselective Introduction of the t-Butoxycarbonyl (BOC) Protective Group at Unhindered Amines: Application to Aminoglycoside Chemistry, J. Org. Chem. 1994, 59, 1918.

25. Imtiaz, U.; Manavathu, E. K.; Mobashery; S.; Lerner, S. A. Reversal of Clavulanate

Resistance Conferred by a Ser-244 Mutant of the TEM-1 β-Lactamase as a Result of a Second Mutation (Arg to Ser at Position 164) That Enhances Activity Against Ceftazidime, Antimicrob. Agents Chemother. 1994, 38, 1134.

26. Imtiaz, U.; Billings, E. M.; Knox, J. R.; Mobashery, S. A Structure-Based Analysis of the

Inhibition of Class A β-Lactamases by Sulbactam, Biochemistry 1994, 33, 5728. 27. Kocs, R.; Roestamadji, J.; Mobashery, S. A Convenient Triphosgene-Mediated Synthesis

of Symmetric Carboxylic Acid Anhydrides, J. Org. Chem.1994, 59, 2913. 28. Ghosh, S. S.; Said-Nejad, O.; Mobashery, S. A Rational Approach for the Design of

Mechanism-Based Inactivators for Zinc Proteases, Peptides: Chemistry, Structure and Biology, Hodges, R. S. and Smith, J. A. (Eds.), 1994, 607.

29. Tanaka,Y.; Grapsas, I.; Dakoji, S.; Cho, Y.J.; Mobashery, S. Conscripting the Active-Site

Zinc Ion in Carboxypeptidase A in Inactivation Chemistry by a New Type of Irreversible Enzyme Inactivator, J. Am. Chem. Soc. 1994, 116, 7475.


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30. Roestamadji, J.; Mobashery, S. Bis(trichloromethyl)carbonate (triphosgene), Encyclopedia of Reagents for Organic Synthesis, Paquette, L. A. (Editor-in-Chief), 1995 , 575.

31. Grapsas, I.; Mobashery, S. Glyoxylyl Chloride p-Toluenesulfonyl Hydrazone,

Encyclopedia of Reagents for Organic Synthesis, Paquette, L. A. (Editor-in-Chief), 1995, 2624.

32. Taibi, P.; Mobashery, S. (Methylcarboxysulfamoyl)triethylammoium Hydroxide (Burgess

Reagent) Encyclopedia of Reagents for Organic Synthesis, Paquette, L. A. (Editor-in-Chief), 1995, 3345.

33. Grapsas, I.; Mobashery, S. t-Butoxycarbonylimidazole, Encyclopedia of Reagents for

Organic Synthesis, Paquette, L. A. (Editor-in-Chief), 1995 , 835. 34. Grapsas, I.; Mobashery, S. 1-t-Butoxycarbonyl-1,2,4-triazole, Encyclopedia of Reagents for

Organic Synthesis, Paquette, L. A. (Editor-in-Chief), 1995, 843. 35. Grapsas, I.; Mobashery, S. 1-N-(t-Butoxycarbonyl)-1H-benzotriazole-3-N-oxide,

Encyclopedia of Reagents for Organic Synthesis, Paquette, L. A. (Editor-in-Chief), 1995, 833.

36. Siregar, J.J.; Mobashery, S. Methoxycarbonylsulfamoyl chloride, Encyclopedia of

Reagents for Organic Synthesis, Paquette, L. A. (Editor-in-Chief), 1995, 3344. 37. Roestamadji, J.; Grapsas, I.; Mobashery, S. Mechanism-Based Inactivation of Bacterial

Aminoglycoside 3'-phosphotransferases, J. Am. Chem. Soc. 1995, 117, 80. 38. Bulychev, A.; Massova, I.; Lerner, S.A.; Mobashery, S. Penem BRL 42715: An Effective

Inactivator for β-Lactamases, J. Am. Chem. Soc. 1995, 117, 4797. 39. Bulychev, A.; O'Brien, M.E.; Massova, I.; Teng, M.; Gibson, T.A.; Miller, M.J.;

Mobashery, S. Potent Mechanism-Based Inhibition of the TEM-1 β-Lactamase by Novel N-Sulfonyloxy β-Lactams, J. Am. Chem. Soc. 1995, 117, 5938.

40. Taibi, P.; Mobashery, S. Mechanism of Turnover of Imipenem by the TEM β-Lactamase

Revisited, J. Am. Chem. Soc. 1995, 117, 7600. 41. Miyashita, K.; Mobashery, S. Mechanistic Support for the Stepwise Process for

Inactivation of Class A β-Lactamases by Clavulanate, Bioorg. Med. Chem. Lett. 1995, 5, 1043.

42. Fridman, R.; Toth, M.; Pena, D.; Mobashery, S. Activation of Progelatinase B (MMP-9)

by Gelatinase A (MMP-2), Cancer Res. 1995 , 55, 2548. 43. Vakulenko, S. B.; Taibi, P.; Toth, M.; Mobashery, S.; Lerner, S. A. Effect of Asp-179

Mutations in TEMpUC19 β-Lactamase on Susceptibility to β-Lactamase, Antimicrob. Agents Chemother. 1995, 39, 1878.

44. Siregar, J.J.; Miroshnikov, K.; Mobashery, S. Purification, Characterization and

Investigation of Mechanism of Aminoglycoside 3'-Phosphotransferase Type Ia, Biochemistry 1995, 34, 12681.


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45. Roestamadji, J.; Grapsas, I.; Mobashery, S. Loss of Individual Electrostatic Interactions between Aminoglycoside Antibiotics and Resistance Enzymes as an Effective Means to Overcoming Bacterial Drug Resistance, J. Am. Chem. Soc. 1995, 117, 11060.

46. Miyashita, K.; Massova, I.; Taibi, P.; Mobashery, S. Design, Synthesis and Evaluation of a

Potent Mechanism-Based Inhibitor for the TEM β-lactamase with Implications for the Enzyme Mechanism, J. Am. Chem. Soc. 1995, 117, 11055.

47. Miyashita, K.; Massova, I.; Mobashery, S. Quantification of the Extent of Attenuation of

the Rate of Turnover Chemistry of the TEM-1 β-Lactamase by the α-1R-Hydroxyethyl Group in Substrates, Bioorg. Med. Chem. Lett., 1996, 6, 319.

48. Ghosh, S.S.; Dakoji, S.; Tanaka, Y.; Cho, Y.J.; Mobashery, S. Properties of Analogs of an

Intermediate in the Process of Mechanism-Based Inactivation of Carboxypeptidase A, Bioorganic Med. Chem. 1996, 4, 1487.

49. McKay, G. A.; Roestamadji, J.; Mobashery, S.; Wright, G. D. Recognition of

Aminoglycoside Antibiotics by the Enterococcal/Staphylococcal Aminoglycoside 3'-Phosphotransferase Type IIIa: Role of Substrate Amino Groups, Antimicrob. Agents Chemother. 1996, 40, 2648.

50. Maveyraud, L; Massova, I.; Birck, C.; Miyashita, K.; Samama, J. P.; Mobashery, S.

Crystal Structure of 6α-Hydroxymethylpenicillanate Complexed to the TEM-1 β-Lactamase from Escherichia coli: Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided Process J. Am. Chem. Soc. 1996, 118 , 7435.

51. Taibi,P.; Massova, I.; Vakulenko, S.B.; Lerner, S.A.; Mobashery, S. Evidence for

Structural Elasticity of β-Lactamases in the Course of Catalytic Turnover of the Novel Cephalosporin Cefepime, J. Am. Chem. Soc. 1996, 118 , 7441.

52. Massova, I.; Martin, P.; de Mel, S.; Tanaka, Y.; Edwards, B.; Mobashery, S.

Crystallographic and Computational Insight on the Mechanism of Zinc-Ion-Dependent Inactivation of Carboxypeptidase A by 2-Benzyl-3-Iodopropanoate, J. Am. Chem. Soc. 1996, 118 , 12479.

53. Azucena, E.; Grapsas, I.; Mobashery, S. Properties of a Bifunctional Bacterial Antibiotic

Resistance Enzyme That Catalyzes ATP-Dependent 2''-Phosphorylation and Acetyl-CoA-Dependent 6'-Acetylation of Aminoglycosides, J. Am. Chem. Soc. 1997, 119, 2317.

54. Massova, I. ; Fridman, R.; Mobashery, S. Structural Insights into the Catalytic Domains of

Human Matrix Metalloprotease-2 and Human Matrix Metalloprotease-9: Implications for Substrate Specificities, J. Mol. Mod. 1997, 3, 17.

55. Massova, I.; Mobashery, S. Molecular Bases for Interactions between β-Lactam

Antibiotics and β-Lactamases, Acct. Chem. Res. 1997, 30, 162. 56. Bulychev, A.; Massova, I.; Miyashita, K.; Mobashery, S. Nuances of Mechanisms and

Their Implications for Evolution of the Versatile β-Lactamase Activity: from Biosynthetic Enzymes to Drug Resistance Factors, J. Am. Chem. Soc. 1997, 119, 7619.

57. Olson, M. W.; Gervasi, D. C.; Mobashery, S.; Fridman, R. Kinetic Analysis for the

Binding of the Latent and Active Forms of the Human Matrix metalloprotease-2 and -9 to TIMP-1 and TIMP-2, J. Biol. Chem. 1997, 272, 29975.


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58. Massova, I.; Pirkle, H.; Edwards, B. F. P.; Mobashery, S. Insight into the Three-Dimensional Structure of Crotalase: Implications for Biological Activity and Substrate Specificity, Bioorg. Med. Chem. Lett. 1997, 7, 3139.

59. Massova, I; Mobashery, S. Kinship and Diversification of Bacterial Penicillin-Binding

Proteins and β-Lactamases, Antimicrob. Agents Chemother. 1998, 42, 1. 60. Hsu-Chou, R. S. Y.; Mobashery, S.; Yen, T. F. Denitrogenation of Shale Oil by Oxime

Formation from Pyrroles, Energy Sources 1998, 20, 857-866. 61. Massova, I.; Kotra, L. P.; Mobashery, S. Structural Insight into the Binding Motifs for

Calcium Ion and the Non-Catalytic Zinc in Matrix Metalloproteases, Bioorganic Med. Chem. Lett. 1998, 8, 853.

62. Grapsas, I.; Mobashery, S. Synthetic Strategies for Regioselective Structural Modifications

of Multifunctional Aminoglycoside Antibiotics, Recent Res. Devel. in Organic Chem. 1998, 1, 469.

63. Grapsas, I.; Massova, I.; Mobashery, S. 1H-NMR Analysis of Copper-Aminoglycoside

Complexes in Solution and Its Implications for Regioselective Modification of Multifunctional Aminoglycoside Antibiotics, Tetrahedron 1998, 54, 7705.

64. Vakulenko, S. B., Geryk, B.; Kotra, L. P.; Mobashery, S.; Lerner, S. A., Selection and

Characterization of β-Lactam/β-Lactamase Inactivator-Resistant Mutants Following PCR Mutagenesis of the TEM-1 β-Lactamase Gene, Antimicrob. Agents Chemother. 1998, 43, 1542.

65. Massova, I.; Kotra, L. P.; Fridman, R.; Mobashery, S. Matrix Metalloproteases:

Structures, Evolution and Diversification, FASEB J. 1998, 12, 1075. 66. Kotra, L. P.; Mobashery, S. β-Lactam Antibiotics, β-Lactamases, and Bacterial Resistance,

Bull. Pasteur Institute 1998, 96, 139. 67. Mourey, L.; Miyashita, K.; Swarén, P.; Bulychev, A.; Samama, J. P.; Mobashery, S.,

Inhibition of the NMC-A β-lactamase by a Penicillanic Acid Derivative, and the Structural Bases for the Increase in Substrate Profile of This Antibiotic Resistance Enzyme, J. Am. Chem. Soc. 1998, 120, 9383.

68. Maveyraud, L.; Mourey, L.; Kotra, L. P.; Pedelacq, J.-D.; Guillet, V.; Mobashery, S.;

Samama, J. P. Structural Basis for Clinical Longevity of Carbapenem Antibiotics in the Face of Challenge by the Common Class A β-lactamases from the Antibiotic-Resistant Bacteria, J. Am. Chem. Soc. 1998, 120, 9748.

69. Massova, I.; Martin, P.; Bulychev, A.; Kocs, R.; Doyle, M.; Edwards, B. F. P.; Mobashery,

S. Templates for Design of Inhibitors for Serine Proteases: Application of the Program DOC to the Discovery of Novel Inhibitors of Thrombin, Bioorg. Med. Chem. Lett. 1998, 8 , 2463.

70. Bush, K.; Mobashery, S. How β-Lactamases Have Driven Pharmaceutical Drug

Discovery: from Mechanistic Knowledge to Clinical Circumvention, Adv. Exp. Med. Biol. 1998, 456, 71-98.

71. Wright, G. D.; Berghuis, A. M.; Mobashery, S. Aminoglycoside Antibiotics: Structures,

Functions and Resistance, Adv. Exp. Med. Biol. 1998, 456, 27-69.


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72. Li, Z. H.; Bulychev, A.; Kotra, L. P.; Massova, I.; Mobashery, S. Hydrogen Bonding and

Attenuation of the Rate of Enzymic Catalysis, J. Am. Chem. Soc. 1998, 120, 13003. 73. Roestamadji, J.; Mobashery, S. The Use of Neamine as a Molecular Template:

Inactivation of Bacterial Antibiotic Resistance Enzyme Aminoglycoside 3’-Phosphotransferase Type IIa, Bioorg. Med. Chem. Lett. 1998, 8, 3483.

74. Yang, Y.; Roestamadji, J.; Mobashery, S.; Orlando, R. The Use of Neamine as a

Molecular Template: Identification of Active Site Residues in the Bacterial Antibiotic Resistance Enzyme Aminoglycoside 3’-Phosphotransferase Type IIa by Mass Spectroscopy, Bioorg. Med. Chem. Lett. 1998, 8 , 3489.

75. Swarén, P.; Massova, I.; Bellettini, J.; Bulychev, A.; Maveyraud, L.; Kotra, L. P.; Miller,

M. J.; Mobashery, S.; Samama, J. P. Elucidation of Mechanism of Inhibition and X-Ray Structure of the TEM-1 β-Lactamase from Escherichia coli inhibited by a N-Sulfonyloxy-β-lactam, J. Am. Chem. Soc. 1999, 121, 5353.

76. Kotra, L.P.; Mobashery, S. Mechanistic and Clinical Aspects of β-Lactams and β-

Lactamases. Arch. Immunol. Ther. Ex. 1999, 47, 211. 77. Swarén, P.;Golemi, D.; Cabantous, S.; Bulychev, A.; Maveyraud, L.; Mobashery, S.;

Samama, J. P. X-Ray Structure of the Asn276Asp Variant of the Escherichia coli TEM-1 β-Lactamase: Direct Observation of Electrostatic Modulation in Resistance to Inactivation by Clavulanic Acid, Biochemistry, 1999, 38, 9570.

78. Bulychev, A.; Mobashery, S. Class C β-Lactamases Operate at the Diffusion Limit for

Turnover of their Preferred Cephalosporin Substrates, Antimicrob. Agents Chemother. 1999, 43, 1743.

79. Vakulenko, S. B.; Taibi-Tronche, P.; Tóth, M.; Massova, I.; Lerner, S. A.; Mobashery, S.

Effects on Substrate Profile by Mutational Substitutions at Positions 164 and 179 of the Class A TEMpUC19 β-Lactamase from Escherichia coli, J. Biol. Chem., 1999, 274, 23052.

80. Mourey, L.; Kotra, L. P.; Bellettini, J.; Bulychev, A.; O’Brien, M.; Miller, M.J.;

Mobashery, S.; Samama, J. P. Inhibition of the Broad-Spectrum NMC-A β-Lactamase from Enterobacter cloacae by Monocyclic β-Lactams, J. Biol. Chem., 1999, 274, 25260.

81. Kotra, L. P.; Golemi, D.; Amro, N. A.; Liu, G. Y.; Mobashery, S., Dynamics of the

Lipopolysaccharide Assembly on the Surface of Eschericchia coli, J. Am. Chem. Soc. 1999, 121, 8707-8711.

82. Massova, I.; Mobashery, S. Structural and Mechanistic Aspects of Evolution of β-

Lactamases and Penicillin-Binding Proteins, Current Pharm. Design 1999, 5, 929-937. 83. Amro, N. A.; Kotra, L. P.; Wadu-Mesthrige, K.; Bulychev, A.; Mobashery, S.; Liu, G-Y.

Structural Basis of the Escherichia coli Outer-Membrane Permeability, Proc. SPIE, 1999, 3607, 108-122.

84. Haddad, J.; Vakulenko, S.; Mobashery, S. An Antibiotic Cloaked by Its Own Resistance

Enzyme, J. Am. Chem. Soc. 1999, 121, 11922-11923. 85. Lee, W. L., Li, Z. H.; Vakulenko, S.; Mobashery, S. A Light-Inactivated Antibiotic, J.

Med. Chem. 2000, 43, 128-132.


11

86. Olson, M. W.; Bernardo, M. M.; Pietila, M.; Gervasi, D. C.; Toth, M.; Kotra, L. P.;

Massova, I.; Mobashery, S.; Fridman, R. Characterization of the Monomeric and Dimeric Forms of Latent and Active Matrix Metalloproteinase-9, J. Biol. Chem., 2000, 275, 2661-2668.

87. Amro, N. A.; Kotra, L. P.; Wadu-Mesthrige, K.; Bulychev, A.; Mobashery, S.; Liu, G. Y.

High-Resolution Atomic Force Microscopy Studies of the Escherichia coli Outer Membrane: Structural Basis for Permeability, Langmuir 2000, 16, 2789-2796.

88. Therrien, C.; Kotra, L. P., Sanschagrin, F.; Mobashery, S.; Levesque, R. C., Evaluation of

Inhibition of Carbenicillin-Hydrolyzing β-Lactamase PSE-4 by the Clinically Used Mechanism-Based Inhibitors, FEBS Letters 2000, 470, 285-292.

89. Kotra, L. P.; Golemi, D.; Vakulenko, S.; Mobashery,S. Bacteria Fight Back, Chemistry &

Industry 2000, 341-344. 90. Kotra, L. P.; Vakulenko, S.; Mobashery, S. From Genes to Sequences to Antibiotics:

Prospects for Future Developments from Microbial Genomics, Microbes Infect. 2000, 2, 651-658.

91. Golemi, D.; Maveyraud, L.; Vakulenko, S.; Tranier, S.; Ishiwata, A.; Kotra, L. P.; Samama,

J. P.; Mobashery, S. The First Structural and Mechanistic Insights for Class D β-Lactamases: Evidence for a Novel Catalytic Process for Turnover of β-Lactam Antibiotics, J. Am. Chem. Soc. 2000, 122, 6132-6133.

92. Brown, S.; Bernardo, M.; Li, Z. H., Kotra, L. P.; Tanaka, Y.; Fridman, R.; Mobashery, S.

Potent and Selective Mechanism-Based Inhibition of Gelatinases, J. Am. Chem. Soc. 2000, 122, 6799-6800.

93. Ishiwata, A.; Kotra, L. P.; Miyashita, K.; Nagase, T.; Mobashery, S. Stereoselective

reduction of α-bromopenicillanates by tributylphosphine, Org. Lett. 2000, 2, 2889-2892. 94. Bulychev, A.; Bellettini, J. R.; O’Brien, M.; Crocker, P. J.; Samama, J. P.; Miller, M. J.;

Mobashery, S. N-Sulfonyloxy-β-Lactam Inhibitors for β-Lactamases, Tetrahedron 2000, 56, 5719-5728.

95. Golemi, D.; Maveyraud, L.; Ishiwata, A.; Tranier, S.; Miyashita, K.; Nagase, T.; Massova,

I.; Mourey, L.; Samama, Jean-Pierre; Mobashery, S., 6-(Hydroxyalkyl)penicillanates as Probes for Mechanisms of β-Lactamases, J. Antibiot. 2000, 53, 1022-1027.

96. Liu, M.; Haddad, J.; Azucena, E.; Kotra, L. P.; Kirzhner, M.; Mobashery, S., Tethered

Bisubstrate Derivatives as Probes for Mechanism and as Inhibitors of Aminoglycoside 3’-Phosphotransferases, J. Org. Chem., 2000, 65, 7422-7431.

97. Kotra, L. P.; Amro, N. A.; Liu, G.; Mobashery, S., Visualizing Bacteria at High Resolution,

ASM News 2000, 66, 675-681. 98. Kotra, L. P.; Haddad, J.; Mobashery, S., Aminoglycoside Antibiotics: Perspectives on

Mechanisms of Action and Resistance and Strategies to Counter Resistance, Antimicrob. Agents Chemother. 2000, 44, 3249-3256.

99. Toth, M.; Bernardo, M. M.; Gervasi, D. C.; Soloway, P. D.; Wang, Z.; Bigg, H. F.; Overall,

C. M.; DeClerck, Y. A.; Tschesche, D.; Cher, M. L.; Brown, S.; Mobashery, S.; Fridman,


12

R., TIMP-2 Acts Synergistically with Synthetic MMP Inhibitors but not with TIMP-4 to Enhance the MT1-MMP-Dependent Activation of Pro-MMP-2, J. Biol. Chem., 2000, 275, 41415-41423.

100. Maveyraud, L.; Golemi, D.; Kotra, L. P.; Tranier, S.; Vakulenko, S.; Mobashery, S.;

Samama, J. P., Insights into class D β-lactamases are revealed by the crystal structure of the Oxa10 enzyme from Pseudomonas aeruginosa, Structure, 2000, 8, 1289-1298.

101. Kotra, L. P.; Mobashery, S., A Renaissance of Interest in Aminoglycoside Antibiotics,

Curr. Org. Chem. 2001, 5, 193-205. 102. Haddad, J.; Kotra, L. P.; Mobashery, S. Aminoglycoside Antibiotics: Structures and

Mechanism of Action, In Glycochemistry: Principles, Synthesis, and Applications, Wang, G., and Bertozzi, C. (Eds.), Marcel Dekker, Inc., NY, 2001, 307-351.

103. Haddad, J.; Liu, M. Z.; Mobashery, S. Methodologies in Syntheses of Aminoglycoside

Antibiotics, In Glycochemistry: Principles, Synthesis, and Applications, Wang, G., and Bertozzi, C. (Eds.), Marcel Dekker, Inc., NY, 2001, 353-424.

104. Lee, W.; McDonough, M. A.; Kotra, L. P.; Li, Z. H.; Silvaggi, N. R.; Takeda, Y.; Kelly, J.

A., Mobashery, S. A 1.2 Å Snapshot of the Final Step of Bacterial Cell Wall Biosynthesis, Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 1427-1431.

105. Kotra, L. P.; Cross, J. B.; Shimura, Y.; Fridman, R.; Schlegel, H. B.; Mobashery, S. Insight

into the Complex and Dynamic Process of Activation of Matrix Metalloproteinases, J. Am. Chem. Soc. 2001, 123, 3108-3113.

106. Kleifeld, O.; Kotra, L. P.; Gervasi, D. C.; Brown, S.; Bernardo, M. M.; Fridman, R.;

Mobashery, S.; Sagi, I. X-Ray Absorption Studies of Human Matrix Metalloproteinase-2 (MMP-2) Bound to a Highly Selective Mechanism-Based Inhibitor: Comparison to the Latent and Active Forms of the Enzyme, J. Biol. Chem., 2001, 276, 17125-17131.

107. Kreidel, S. J.; Chen, E.; Kotra, L. P.; Howard, E. W.; Mobashery, S,; Smith, J. W.

Substrate Hydrolysis by Matrix Metalloproteinase-9, J. Biol. Chem., 2001, 276, 20572-20578.

108. Azucena, E.; Mobashery, S. Aminoglycoside-Modifying Enzymes: Mechanisms of

Catalytic Processes and Inhibition, Drug Resistance Updates 2001, 4, 106-117. 109. Petty, H.; Fernando, M.; Kindzelskii, A. L.; Zarewych, B.; Ksebati, M. B.; Hryhorczuk, L.

M.; Mobashery, S. Identification of Colchicine in Placental Blood from Patients Using Herba Medicines Chem. Res. Toxicol. 2001, 14, 1254-1258.

110. Kim, D. H.; Mobashery, S. Mechanism-Based Inhibition of Zinc Proteases, Curr. Med.

Chem. 2001, 8, 959-965. 111. Nagase, T.; Golemi, D.; Ishiwata, A.; Mobashery, S. Inhibition of β-Lactamases by 6,6-

Bis(hydroxymethyl)penicillanate, Bioorg. Chem. 2001, 29, 140-145. 112. Grapsas, I.; Lerner, S. A.; Mobashery, S., Conjoint Molecules of Cephalosporins and

Aminoglycosides, Arch. Pharm. Pharm. Med. Chem. 2001, 334, 295-301.


13

113. Golemi, D.; Maveyraud, L.; Vakulenko, S.; Samama, J. P.; Mobashery, S. Critical Involvement of a Carbamylated Lysine in Catalytic Function of Class D β-Lactamases, Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 14280-14285.

114. Mobashery, S.; Azucena, E. Bacterial Antibiotic Resistance, In “Encyclopedia Life Sci.”,

London: Nature Publishing Group, UK, 2002, volume 2, pp 472-477 (http://www.els.net). 115. Mobashery, S.; Kotra, L. Transition State Stabilization, In “Encyclopedia Life Sci.”,

London: Nature Publishing Group, UK, 2002, volume 18, pp 466-473 (http://www.els.net). 116. Golemi, D.; Maveyraud, L.; Haddad, J.; Lee, W.; Ishiwata, A.; Miyashita, K.; Mourey, L.;

Vakulenko, S.; Kotra, L. P.; Samama, J. P.; Mobashery, S., Antibacterials as Wonder Drugs and How Their Effectiveness Is Being Compromised, In Trends in Drug Research III, van der Goot, H. (Ed.), Pharmacochemistry Library, Vol. 32, 2002, Elsevier Science, pp193-205.

117. Kotra, L. P.; Samama, J. P.; Mobashery, S. Structural Aspects of β-Lactamase Evolution,

In Bacterial Resistance to Antimicrobials, Mechanisms, Genetics, Medical Practice and Public Health, Lewis, K.; Salyers, A. A.; Haber, H. W.; Wax, R. G., Eds.; Marcel Dekker, Inc, 2002, pp 123-159, New York .

118. Bernardo, M. M.; Brown, S.; Li, Z. H.; Fridman, R.; Mobashery, S. Design, Synthesis and

Characterization of Potent, Slow-Binding Inhibitors that Are Selective for Gelatinases, J. Biol. Chem., 2002, 277, 11201-11207.

119. Maveyraud, L.; Golemi, D.; Ishiwata, A.; Meroueh, O.; Mobashery, S.; Samama, J. P.

High-Resolution X-Ray Structure of an Acyl-Enzyme Species for the Class D OXA-10 β-Lactamase, J. Am. Chem. Soc. 2002, 124, 2461-2465.

120. Haddad, J.; Kotra, L. P.; Llano-Sotelo, B.; Kim, C.; Azucena, E. F.; Liu, M.; Vakulenko, S.

B.; Chow, C. S.; Mobashery, S. Design of Novel Antibiotics that Bind to the Ribosomal Acyltransfer Site, J. Am. Chem. Soc. 2002, 124, 3229-3237.

121. Llano-Sotelo, B.; Azucena, E.; Kotra, L. P.; Mobashery, S.; Chow, C. S. Aminoglycosides

Modified by Resistance Enzymes Display Diminished Binding to the Bacterial Ribosomal Aminoacyl-tRNA Site, Chemistry & Biology, 2002, 9, 455-463.

122. Fuda, C; Vakulenko, S. B.; Golemi, D.; Geryk, B.; Suvorov, M.; Knox, J. R.; Mobashery,

S.; Lerner, S. A., Mutational Replacement of Leu-293 in the Class C Enterobacter cloacae P99 β-Lactamase Confers Decreased Susceptibility to Cefepime, Antimicrob. Agents Chemother. 2002, 46, 1966-1970.

123. Toth, M; Hernandez-Barrantes, S.; Osenkowski, P.; Bernardo, M. M.; Gervasi, D. C.;

Shimura, Y.; Meroueh, O.; Kotra, L. P.; Galvez, B. G.; Arroyo, A. G.; Mobashery, S.; Fridman, R. Complex Pattern of Membrane Type-1 Matrix Metalloproteinase Shedding. Regulation by Autocatalytic Cell Surface Inactivation of Active Enzyme, J. Biol. Chem., 2002, 277, 26340-26350.

124. Meroueh, O.; Roblin, P.; Golemi, D.; Maveryraud, L.; Vakulenko, S. B.; Zhang, Y.;

Samama, J. P.; Mobashery, S. Molecular Dynamics at the Root of Expansion of Function in the M69L Inhibitor-Resistant TEM β-Lactamase from Escherichia coli, J. Am. Chem. Soc. 2002, 124, 9422-9430.


14

125. Kotra, L. P.; Zhang, L.; Fridman, R.; Orlando, R.; Mobashery, S. N-Glycosylation Pattern of the Zymogenic Form of Human Matrix Metalloproteinase-9, Bioorg. Chem. 2002, 30, 356-370.

126. Golemi-Kotra, D.; Mobashery, S. Antibiotic Resistance, Kirk-Othmer Encyclopedia of

Chemical Technology, 4th Edition, John Wiley & Sons, Inc., 2002, http://www.mrw.interscience.wiley.com/kirk/.

127. Fridman, R.; Toth, M.; Chvyrkova, I.; Meroueh, S. O.; Mobashery, S. Cell Surface

Association of Matrix Metalloproteinase-9 (Gelatinase B), Cancer and Metastasis Reviews 2003, 22, 153-166.

128. Wilkinson, A. S.; Bryan, P. K.; Meroueh, S. O.; Page, M. G. P.; Mobashery, S.; Wharton,

C. W. A Dynamic Structure for the Acylenzyme Species of the Antibiotic Aztreonam with the Citrobacter freundii β-Lactamase Revealed by Infrared Spectroscopy and Molecular Dynamics Simulations, Biochemistry 2003, 42, 1950-1957.

129. Russell, R.J.M.; Murray, J.B., Lentzen, G.; Haddad, J.; Mobashery, S. The Complex of a

Designer Antibiotic with a Model Aminoacyl Site of the 30S Ribosomal Subunit Revealed by X-Ray Crystallography, J. Am. Chem. Soc. 2003, 125, 3410-3411.

130. Golemi-Kotra, D.; Vakulenko, S.; Mobashery, S. Evolution of Multiple Mechanisms of

Resistance to β-Lactam Antibiotics; Forum on Emerging Infections "The Resistance Phenomenon in Microbes and Infectious Disease Vectors: Implications for Human Health and Strategies for Containment", Institute of Medicine, National Academy of Sciences 2003, pp160-167.

131. Vakulenko, S. B.; Mobashery, S. Versatility of Aminoglycosides and Prospects for Their

Future, Clin. Microbiol. Rev. 2003, 16, 430-450. 132. Golemi-Kotra, D.; Cha, J. Y.; Meroueh, S. O.; Vakulenko, S. B.; Mobashery, S. Resistance

to β-Lactam Antibiotics and Its Mediation by the Sensor Domain of the Transmembrane BlaR Signaling Pathway in Staphylococcus aureus, J. Biol. Chem. 2003, 278, 18419-18425.

133. Rosenblum, G.; Meroueh, S. O.; Kleifeld, O.; Brown, S.; Singson, S. P.; Fridman, R.;

Mobashery, S.; Sagi, S. Structural Basis for Potent Slow-Binding Inhibition of Human Matrix Metalloproteinase-2 (MMP-2), J. Biol. Chem. 2003, 278, 27009-27015.

134. Richard, J. P.; Mobashery, S. Complex Biological Processes and Their Central Chemical

Events Curr. Opin. Chem. Biol. 2003, 7, 525-527. 135. Meroueh, S. O.; Minasov, G.; Lee, W.; Shoichet, B. K.; Mobashery, S. Structural Aspects

of Evolution of β-Lactamases from Penicillin-Binding Proteins, J. Am. Chem. Soc. 2003, 125, 9612-9618.

136. Lee, M.; Hesek, D.; Suvorov, M.; Lee, W., Vakulenko, S.; Mobashery, S. A Mechanism-

Based Inhibitor Targeting the DD-Transpeptidase Activity of Bacterial Penicillin-Binding Protein, J. Am. Chem. Soc. 2003, 125, 16322-16326.

137. Hesek, D.; Suvorov, M.; Morio, K.; Lee, M.; Brown, S.; Vakulenko, S. B.; Mobashery, S.

Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 (PBP5) of Gram-Negative Bacteria, J. Org. Chem. 2004, 69, 778-784.


15

138. Hesek, D.; Lee, M.; Morio, K.; Mobashery, S. Synthesis of a Fragment of Bacterial Cell Wall J. Org. Chem. 2004, 69, 2137-2146.

139. Lim, I. T.; Brown, S.; Mobashery, S. A Convenient Synthesis of a Selective Gelatinase

Inhibitor as an Antimetastatic Agent J. Org. Chem. 2004, 69, 3572-3573. 140. Kim, C.; Haddad, J.; Vakulenko, S. B.; Meroueh, S. O.; Wu, Y.; Yan, H.; Mobashery, S.

Fluorinated Aminoglycosides and Their Mechanistic Implication for Aminoglycoside Phosphotransferases from Gram-Negative Bacteria Biochemistry 2004, 43, 2373-2383.

141. Brown, S.; Meroueh, S. O.; Fridman, R.; Mobashery, S. Quest for Selectivity in Inhibition

of Matrix Metalloproteinases, Curr.Topics Med. Chem. 2004, 4, 1227-1238. 142. Cha, J. Y.; Ishiwata, A.; Mobashery, S. A Novel β-Lactamase Activity from a Penicillin-

Binding Protein of Treponema pallidum and Why Syphilis Is Still Treatable with Penicillin J. Biol. Chem. 2004, 279, 14917-14921.

143. Solomon, A.; Rosenblum, G.; Gonzales, P. E.; Leonard, J. D.; Mobashery, S.; Milla, M. E.;

Sagi, I. Pronounced Diversity in Electronic and Chemical Properties between the Catalytic Zinc Sites of TACE and MMPs Despite Their High Structural Similarity, J. Biol. Chem. 2004, 279 31646-31654.

144. Kim, D. H.; Mobashery, S. Mechanism-Based Inhibition of Metalloproteinases, Frontiers

Med. Chem. 2004, 8, 959-965. 145. Golemi-Kotra, D.; Meroueh, S. O.; Kim, C.; Vakulenko, S. B.; Bulychev, A.; Stemmler, A.

J.; Stemmler, T. L., Mobashery, S. The Importance of a Critical Protonation State and the Fate of the Catalytic Steps in Class A β-Lactamases and Penicillin-Binding Proteins, J. Biol. Chem. 2004, 279, 34665-34673.

146. Fuda, C.; Suvorov, M.; Vaklenko, S. B.; Mobashery, S. The Basis for Resistance to β-

Lactam Antibiotics by Penicillin-Binding Protein 2a (PBP2a) of Methicillin-Resistant Staphylococcus aureus, J. Biol. Chem. 2004, 279, 40802-40806.

147. Lim, I. T.; Meroueh. S. O.; Lee, M.; Heeg, M. J.; Mobashery, S. A New Strategy in

Inhibition of Cathepsin B, A Target in Tumor Invasion and Metastasis, J. Am. Chem. Soc. 2004, 126, 10271-10277.

148. Lee, M.; Fridman, R.; Mobashery, S. Extracellular Proteases as Targets for Treatment of

Cancer Metastases Chem. Soc. Rev. 2004, 33, 401-409. 149. Birck, C.; Cha, J. Y.; Cross, J.; Schulze-Briese, C.; Meroueh, S. O.; Schlegel, H. B.;

Mobashery, S.; Samama, Jean-Pierre The X-Ray Crystal Structure of the Acylated β-Lactam Sensor Domain of BlaR1 from Staphylococcus aureus and the Mechanism of Receptor Activation for Signal Transduction, J. Am. Chem. Soc. 2004, 126, 13945-13947.

150. Lee, M.; Hesek, D.; Mobashery, S. A Practical Synthesis of Nitrocefin, J. Org. Chem.

2004, 70, 367-369. 151. Fisher, J. F.; Meroueh, S. O.; Mobashery, S. Bacterial Resistance to β-Lactam Antibiotics:

Compelling Opportunism, Compelling Opportunity, Chem. Rev. 2005, 105, 395-424.


16

152. Fuda, C.; Hesek, D.; Lee, M.; Morio, K.; Nowak, T.; Mobashery, S. Activation for Catalysis of Penicillin-Binding Protein 2a (PBP2a) from Methicillin-Resistant Staphylococcus aureus by Bacterial Cell Wall, J. Am. Chem. Soc. 2005, 127, 2056-2057.

153. Krüger, A.; Arlt, M. J. E.; Gerg, M.; Kopitz, C.; Bernardo, M. M.; Chang, M.; Mobashery,

S.; Fridman, R. Antimetastatic Activity of a Novel Mechanism-Based Gelatinase Inhibitor, Cancer Res. 2005, 65, 4523-4526.

154. Toth, M.; Osenkowski, P.; Hesek, D.; Brown, S.; Meroueh, S.; Sakr, W.; Mobashery, S.;

Fridman, R. Cleavage at the Stem Region Releases an Active Ectodomain of the Membrane Type 1-Matrix Metalloproteinase, Biochem. J. 2005, 387, 497-506.

155. Kim, C. Mobashery, S. Phosphoryl Transfer by Aminolgycoside 3'-Phosphotransferases

and Manifestation of Antibiotic Resistance, Bioorg. Chem. 2005, 33, 149-158. 156. Cross, J. B.; Vreven, T.; Meroueh, S. O.; Mobashery, S.; Schlegel, H. B. Computational

Investigation of Irreversible Inactivation of the Zinc-Dependent Protease Carboxypeptidase A, J. Phys. Chem. B 2005, 109, 4761-4769.

157. Thomas, V. L.; Golemi-Kotra, D.; Kim, C.; Vakulenko, S. B.; Mobashery, S.; Shoichet, B.

K. Structural Consequences of the Inhibitor-Resistant Ser130Gly Substitution in TEM β-Lactamase, Biochemistry 2005, 44, 9330-9338.

158. Ikejiri, M.; Bernardo, M.; Meroueh, S. O.; Brown, S.; Chang, M. Fridman, R.; Mobashery,

S. Design, Synthesis and Evaluation of a Mechanism-Based Inhibitor for Gelatinase A, J. Org. Chem. 2005, 70, 5709-5712.

159. Gu, Z.; Cui, J.; Brown, S.; Fridman, R.; Mobashery, S.; Strongin, A. Y.; Lipton, S. A. A

Highly Specific Inhibitor of Matrix Metalloproteinase-9 Rescues Laminin from Proteolysis and Neurons from Apoptosis in Transient Focal Cerebral Ischemia, J. Neurosci. 2005, 25, 6401-6408.

160. Osenkowski, P.; Meroueh, S. O.; Pavel, D.; Mobashery, S.; Fridman, R. Mutational and

Structural Analyses of the Hinge Region of Membrane Type 1-Matrix Metalloproteinase and Enzyme Processing, J. Biol. Chem. 2005, 280, 26160-26168.

161. Lee, M.; Bernardo, M. M.; Meroueh, S. O.; Brown, S.; Fridman, R.; Mobashery, S.

Synthesis of Chiral 2-(4-Phenoxyphenylsulfonylmethyl)-thiiranes as Selective Gelatinase Inhibitors. Org. Lett. 2005, 7, 4463-4465.

162. Li, J.; Cross, J. B.; Vreven, T.; Meroueh, S. O.; Mobashery, S.; Schlegel, H. B. A

Theoretical Study of Lysine Carboxylation in Proteins: OXA-10 β-Lactamase, Proteins: Structure, Function, and Bioinformatics 2005, 61, 246-257.

163. Ikejiri, M.; Bernardo, M. M.; Bonfil, R. D.; Toth, M.; Chang, M.; Fridman, R.; Mobashery,

S. Potent Mechanism-Based Inhibitors for Matrix Metalloproteinases, J. Biol. Chem. 2005, 280, 33992-34002.

164. Meroueh, S. O.; Fisher, J. F.; Schlegel, H. B.; Mobashery, S. The Ab Initio QM/MM Study

of Class A β-Lactamase Acylation: Dual Participation of Glu166 and Lys73 in a Concerted Base Promotion of Ser70, J. Am. Chem. Soc. 2005, 127, 15397-15407.

165. Fuda, C. C. S., Fisher, J. F.; Mobashery, S. β-Lactam Resistance in Staphylococcus aureus:

The Adaptive Resistance of a Plastic Genome, Cell. Molec. Life Sci. 2005, 62, 2617-2633.


17

166. Murray, J. B.; Meroueh, S. O.; Russell, R. J. M.; Lentzen, G.; Haddad, J.; Mobashery, S.

Interactions of Designer Antibiotics and the Bacterial Ribosomal Aminoacyl-tRNA Site, Chemistry & Biology 2006, 13, 129-138.

167. Kim, C.; Cha, J. Y.; Yan, H.; Vakulenko, S. B.; Mobashery, S. Hydrolysis of ATP by

Aminoglycoside 3’-Phosphotransferases: An Unexpected Cost to Bacteria for Harboring an Antibiotic Resistance enzyme, J. Biol. Chem. 2006, 281, 6964-6969.

168. Meroueh, S. O.; Bencze, K. Z.; Hesek, D.; Lee, M.; Fisher, J. F.; Stemmler, T. L.;

Mobashery, S. Three-Dimensional Structure of the Bacterial Cell Wall Peptidoglycan, Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 4404-4409.

169. Bonfil, R. D.; Sabbota, A.; Nabha, S.; Bernardo, M. M.; Dong, Z.; Meng, H.; Yamamoto,

H.; Chinni, S. R.; Lim, I. T.; Chang, M.; Filetti, L. C.; Mobashery, S.; Cher, M. L.; Fridman, R. Inhibition of Human Prostate Cancer Growth, Osteolysis and Angiogenesis in a Bone Metastasis Model by a Novel Mechanism-Based Selective Gelatinase Inhibitor, Int. J. Cancer 2006, 118, 2721-2726.

170. Fisher, J. F.; Mobashery, S. Recent Advances in MMP Inhibitor Design, Cancer Metastasis

Rev., 2006, 25, 115-136. 171. Hesek, D.; Noll, B. C.; Mobashery, S. Side Reaction of Significance in Preparation of

Peptide- or Peptidomimetic-Based Hydroxamate Enzyme Inhibitors, J. Org. Chem. 2006, 71, 2885-2887.

172. Fuda, C.; Hesek, D.; Lee, M.; Heilmayer, W.; Novak, R.; Vakulenko, S. B.; Mobashery, S.

Mechanistic Basis for the Action of New Cephalosporin Antibiotics Effective Against Methicillin- and Vancomycin-Resistant Staphylococcus aureus, J. Biol. Chem. 2006, 281, 10035-10041.

173. Hesek, D.; Toth, M.; Meroueh, S. O.; Brown, S.; Zhao, H.; Sakr, W.; Fridman, R.;

Mobashery, S. Design and Characterization of a Metalloproteinase Inhibitor-Tethered Resin for the Detection of Active MMPs in Biological Samples, Chemistry & Biology 2006, 13, 379-386.

174. Rekharsky, M.; Hesek, D.; Lee, M.; Meroueh, S. O.; Inoue, Y.; Mobashery, S.

Thermodynamics of Interactions of Vancomycin and Synthetic Surrogates of Bacterial Cell Wall, J. Am. Chem. Soc. 2006, 128, 7736-7737.

175. Thumanu, K.; Cha, Y.; Fisher, J. F.; Perrins, R.; Mobashery, S.; Wharton, C. The Discrete

Steps in Sensing of β-Lactam Antibiotics by the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus bacterium Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 10630-10635.

176. Kim, C.; Hesek, D.; Zajíček, J.; Vakulenko, S. B.; Mobashery, S. Characterization of the

Bifunctional Aminoglycoside-Modifying Enzyme ANT(3’’)-Ii/AAC(6’)-IId from Serratia marcescens, Biochemistry, 2006, 45, 8368-8377.

177. Hesek, D.; Toth, M. Krchnak, V.; Fridman, R.; Mobashery, S. Synthesis of an Inhibitor-

Tethered Resin for Detection of Active Matrix Metalloproteinases Involved in Disease, J. Org. Chem. 2006, 71, 5848-5854.

178. Fisher, J. F.; Meroueh, S. O.; Mobashery, S. Nanomolecular and Supramolecular Paths

toward the Bacterial Peptidoglycan Structure, Microbe, 2006, 1, 420-427.


18

179. Chang, M.; Mobashery, S. Academic Laboratory as a Small Pharmaceutical Company,

Medchem News (Japan), 2006, 16, 8-12. 180. Toth, M.; Sohail, A.; Mobashery, S.; Fridman, R. MT1-MMP Shedding Involves an

ADAM and Is Independent of Its Localization in Lipid Rafts, Biochem. Biophys. Res. Comm. 2006, 350, 377-384.

181. Rosenberg, G. A.; Estrada, E. Y.; Mobashery, S. Effect of Synthetic Matrix

Metalloproteinase Inhibitors on Lipopolysaccharide-Induced Blood-Brain Barrier Opening in Rodents: Differences in Response Based on Strains and Solvent, Brain Research 2006, 1133, 186-192.

182. Meroueh, S. O.; Cha, J.; Mobashery, S. Inhibition of Class A β-Lactamases, In Enzyme-

Mediated Resistance to Antibiotics: Mechanisms, Dissemination, and Prospects for Inhibition, Bonomo, R. A.; Tolmasky, M. E., Eds.; ASM Press, 2007, pp101-114, Washington D.C.

183. Kling, D.; Chow, C.; Mobashery, S. Binding of Antibiotics to the Aminoacyl-tRNA Site of

Bacterial Ribosome, in Aminoglycoside Antibiotics: From Chemical Biology to Drug Discovery, Second Edition, Dev P. Arya, Ed., John Wiley & Sons, Inc, 2007, 225-233.

184. Cha, J.; Mobashery, S. Lysine Nζ-Decarboxylation in the BlaR1 Protein from

Staphylococcus aureus at the Root of Its Function As an Antibiotic Sensor, J. Am. Chem. Soc. 2007, 129, 3834-3835.

185. Kim, C.; Villegas-Estrada, A.; Hesek, D.; Mobashery, S. Mechanistic Characterization of

the Bifunctional Aminoglycoside-Modifying Enzyme AAC(3)-Ib/AAC(6ʹ)-Ibʹ from Pseudomonas aeruginosa, Biochemistry 2007, 46, 5270-5282.

186. Toth, M.; Zajicek, J.; Kim, C.; Chow, J. W.; Smith, C.; Mobashery, S.; Vakulenko, S.

Kinetic Mechanism of Enterococcal Aminoglycoside Phosphotransferase 2’’-Ib, Biochemistry 2007, 46, 5570-5578.

187. Cho, S.; Wang, Q.; Swaminathan, C. P.; Hesek, D.; Lee, M.; Boons, G. J.; Mobashery, S.;

Mariuzza, R. A. Structural Insights into the Bactericidal Mechanism of Human Peptidoglycan Recognition Proteins, Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 8761-8766.

188. Meroueh, S. O.; Mobashery, S. Conformational Transition in the Aminoacyl t-RNA Site of

the Bacterial Ribosome both in the Presence and Absence of an Aminoglycoside Antibiotic Chem. Biol. Drug Design 2007, 69, 291-297.

189. Bonfil, R. D.; Dong, Z.; Trindade Filho, J. C.; Sabbota, A.; Osenkowski, P.; Nabha, S.;

Yamamoto, H.; Chinni, S. R.; Zhao, H.; Mobashery, S.; Vessella, R. L.; Fridman, R.; Cher, M. L. Prostate Cancer-Associated Membrane Type 1-Matrix Metalloproteinase: Its Pivotal Role in Bone Response and Intraosseous Tumor Growth, Am. J. Pathol. 2007, 170, 2100-2111.

190. Kling, D.; Hesek, D.; Shi, Q.; Mobashery, S. Design and Synthesis of a Structurally

Constrained Aminoglycoside, J. Org. Chem. 2007, 72, 5450-5453. 191. Cha, J.; Vakulenko, S. B.; Mobashery, S. Characterization of the β-Lactam Antibiotic

Sensor Domain of the MecR1 Signal Sensor/Transducer Protein from Methicillin-Resistant Staphylococcus Aureus, Biochemistry 2007, 46, 7822-7831.


19

192. Fuda, C.; Suvorov, M.; Shi, Q.; Hesek, D.; Lee, M.; Mobashery, S. Shared Functional

Attributes between the mecA Gene Product of Staphylococcus sciuri and Penicillin-Binding Protein 2a of Methicillin-Resistant Staphylococcus Aureus, Biochemistry 2007, 46, 8050-8057.

193. Suvorov, M.; Vakulenko, S. B.; Mobashery, S. Cytoplasmic Membrane Anchoring of a

Class A β-Lactamase and Its Capacity in Manifesting Antibiotic Resistance, Antimicrob. Agents Chemother. 2007, 51, 2937-2942.

194. Perez-Dorado, I.; Campillo, N. E.; Monterroso, B.; Hesek, D.; Lee, M.; Paez, J. A.; Garcia,

P.; Martinez-Ripoll, M.; Garcia, J. L.; Mobashery, S.; Menendez, M.; Hermoso, J. A. Elucidation of the Molecular Recognition of Bacterial Cell Wall by Modular Pneumococcal Phage Endolysin Cpl-1, J. Biol. Chem. 2007, 282, 24990-24999.

195. Zhang, W.; Shi, Q.; Meroueh, S. O., Vakulenko, S. B.; Mobashery, S. Catalytic Mechanism

of Penicillin-Binding Protein 5 of Escherichia Coli, Biochemistry 2007, 46, 10113-10121. 196. Lee, M.; Villegas-Estrada, A.; Celenza, G.; Boggess, B.; Toth, M.; Kreitinger, G.; Forbes,

C.; Fridman, R.; Mobashery, S.; Chang, M. Metabolism of a Highly Selective Gelatinase Inhibitor Generates Active Metabolite, Chem. Biol. Drug Design 2007, 70, 371-382.

197. Rosenblum, G.; Meroueh, S.; Toth, M.; Fisher, J. F.; Fridman, R.; Mobashery, S.; Sagi, I.

Molecular Structures and Dynamics of the Stepwise Activation of a Matrix Metalloproteinase Zymogen: Challenging the Cysteine Switch Dogma, J. Am. Chem. Soc. 2007, 129, 13566-13574.

198. Brickner, S. J.; Mobashery, S. Prospects of Therapies Targeting Resistant Bacteria—New

Challenges Twenty Years Post Emergence of Vancomycin-Resistant Enterococcus, Curr. Opin. Microbiol. 2007, 10, 425-427.

199. Cha, J. Y.; Kotra, L. P.; Mobashery, S. Resistance to β-Lactam Antibiotics Mediated by β-

Lactamases: Structure, Mechanism and Evolution, In Bacterial Resistance to Antimicrobials, Second Edition, Wax, R. G.; Lewis, K.; Salyers, A. A.; Haber, H. W., Eds.; CRC Press, Inc, 2008, pp 103-132, Boca Raton.

200. Bonfil, R. D.; Fridman, R.; Mobashery, S.; Cher, M. L. Are Matrix Metalloproteinases

Relevant Therapeutic Targets for Prostate Cancer Bone Metastasis?, Current Oncology 2008, 15, 23-28.

201. Kim, D. H.; Lilliehook, C.; Roides, B.; Chen, Z.; Chang, M.; Mobashery, S.; Goldman, S.

A. Testostrone-Induced MMP-Activation Is a Checkpoint for Neuronal Addition to the Adult Songbird Brain, J. Neurosci. 2008, 28, 208-216.

202. Celenza, G.; Villegas-Estrada, A.; Lee, M.; Boggess, B.; Forbes, C.; Wolter, W. R.;

Suckow, M. A.; Mobashery, S.; Chang, M. Metabolism of (4-Phenoxyphenylsulfonyl)-methylthiirane, a Selective Gelatinase Inhibitor, Chem. Biol. Drug Design 2008, 71, 187-196.

203. Totir, M. A., Cha, J.; Ishiwata, A.; Wang, B.; Sheri, A.; Anderson, V. E.; Buynak, J.;

Mobashery, S.; Carey, P. R. Why Clinically Used Tazobactam and Sulbactam Are Poor Inhibitors of OXA-10 β-Lactamase: Raman Crystallographic Evidence, Biochemistry 2008, 47, 4094-4101.


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204. Badarau, A.; Shi, Q.; Chow, J. W.; Zajicek, J.; Mobashery, S.; Vakulenko, S. Aminoglycoside 2’’-Phosphotransferase Type IIIa from Enterococcus, J. Biol. Chem. 2008, 283, 7638-7647.

205. Lemaire, S.; Fuda, C.; Van Bambeke, F.; Tulkens, P. M.; Mobashery, S. Restoration of

Susceptibility of Methicillin-Resistant Staphylococcus aureus (MRSA) to β-Lactam Antibiotics by Acidic pH: Role of Penicillin-Binding Protein 2A (PBP 2A), J. Biol. Chem. 2008, 283, 12769-12776.

206. Lee, M.; Hesek, D.; Shi, Q.; Noll, B. C.; Fisher, J. F.; Chang, M.; Mobashery, S.

Conformational Analyses of Thiirane-Based Gelatinase Inhibitors, Bioorg. Med. Chem. Lett. 2008, 18, 3064-3067.

207. Martin, M. D.; Carter, K. J.; Jean-Philippe, S.; Chang, M.; Mobashery, S.; Thiolloy, S.;

Lynch, C. C.; Matrisian, L. M.; Fingleton, B. Effect of Ablation or Inhibition of MMP9 on Pulmonary Metastasis in a Breast Cancer Model Is Dependent on Genetic Background, Cancer Res. 2008, 68, 6251-6259.

208. Lee, M.; Hesek, D.; Mobashery, S. Synthetic Efforts in Preparations of Components of the

Bacterial Cell Wall, In Chemical Glycobiology, ACS Press, 2008, pp54-78, Washington, DC.

209. Villegas-Esterada, A.; Lee, M.; Hesek, D.; Vakulenko, S. B.; Mobashery, S. Co-opting the

Cell Wall in Fighting Methicillin-Resistant Staphylococcus aureus: Potent Inhibition of PBP 2a by Two Anti-MRSA β-Lactam Antibiotics, J. Am. Chem. Soc. 2008, 130, 9212-9213.

210. Shi, Q.; Meroueh, S. O.; Fisher, J. F.; Mobashery, S. Investigation of the Mechanism of the

Cell Wall DD-Carboxypeptidase Reaction of Penicillin-Binding Protein 5 of Escherichia coli by QM/MM Calculations, J. Am. Chem. Soc. 2008, 130, 9293-9303.

211. Suvorov, M.; Lee, M.; Hesek, D.; Boggess, B.; Mobashery, S. Lytic Transglycosylase

MltB of Escherichia coli and Its Role in Recycling of Peptidogycan Strands of Bacterial Cell Wall, J. Am. Chem. Soc. 2008, 130, 11878-11879.

212. Hesek, D.; Lee, M.; Yamaguchi, T.; Noll, B.; Mobashery, S. A Facile Preparation of a

Highly Functionalized Tetrahydropyran by Catalytic Hydrogenation of an Oxazoline, J. Org. Chem. 2008, 73, 7349-7352.

213. Zhao, H.; Sohail, A.; Sun, Q.; Shi, Q.; Kim, S.; Mobashery, S.; Fridman, R. Identification

and Role of the Homodimerization Interface of the GPI-Anchored MMP25 (MT6-MMP), J. Biol. Chem. 2008, 283, 35023-35032.

214. Suvorov, M.; Fisher, J. F.; Mobashery, S. Bacterial Cell Wall: Morphology and

Biochemistry, Pract. Handb. Microbiol. (2nd Ed.) 2009, 153-183. 215. Lee, M.; Celenza, G.; Boggess, B.; Blase, J.; Shi, Q.; Toth, M.; Bernardo, M. M.; Wolter,

W. R.; Suckow, M. A.; Hesek, D.; Noll, B. C.; Fridman, R.; Mobashery, M.; Chang, M., A Potent Gelatinase Inhibitor with Anti-tumor-invasive Activity and Its Metabolic Disposition, Chem. Biol. Drug Design 2009, 73, 189-202.

216. Hesek, D.; Lee, M.; Noll, B.; Fisher, J.; Mobashery, S. Complications from Dual Roles of

Sodium Hydride as a Base and as a Reducing Agent, J. Org. Chem. 2009, 74, 2567-2570.


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217. Toth, M.; Chow, J. W.; Mobashery, S.; Vakulenko, S. B. Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2"-phosphotransferases, J. Biol. Chem. 2009, 284, 6690-6696.

218. Molina, R.; Gonzalez, A.; Stelter, M.; Perez-Dorado, I., Kohn, R.; Morales, M.;

Campuzano, S.; Campillo, N. E.; Mobashery, S.; Garcia, J. L.; Garcia, P.; Hermoso, J. A. Crystal Structure of Cbpf, a Bifunctional Choline-Binding Protein and Autolysis Regulator from Streptococcus pneumoniae, EMBO Rep. 2009, 10, 246-251.

219. Hesek, D.; Lee, M.; Zhang, W.; Noll, B. C.; Mobashery, S. Total Synthesis of N-

Acetylglucosamine-1,6-anhydro-N-acetylmuramylpentapeptide and Evaluation of Its Turnover by AmpD from Escherichia coli, J. Am. Chem. Soc. 2009, 131, 5187-5193.

220. Lee, M.; Zhang, W.; Hesek, D.; Noll, B. C., Boggess, B.; Mobashery, S. Bacterial AmpD at

the Crossroads of Peptidoglycan Recycling and Manifestation of Antibiotic Resistance, J. Am. Chem. Soc. 2009, 131, 8742-8743.

221. Testero, S. A.; O'Daniel, P. I.; Shi, Q.; Lee, M.; Hesek, D.; Ishiwata, A.; Noll, B. C.;

Mobashery, S. Regiospecific Syntheses of 6α-(1R-hydroxyoctyl)penicillanic acid and 6β-(1R-hydroxyoctyl)penicillanic acid and Mechanistic Probes of Class D β-Lactamases, Org. Lett. 2009, 8, 2515-2518.

222. Tao, P.; Fisher, J. F.; Mobashery, S.; Schlegel, H. B. DFT Studies of the Ring-Opening

Mechanism of SB-3CT, a Potent Inhibitor of Matrix Metalloproteinase 2, Org. Lett. 2009, 11, 2559-2562.

223. Lee, M.; Hesek, D.; Noll, B. C.; Mobashery, S. Side Reaction Due to Reactivity of

Dimethylmaleoyl (DMM) Moiety as Amine Protective Group, Chem. Pap. 2009, 63, 592-597.

224. Llarrull, L. I.; Fisher, J. F.; Mobashery, S. Molecular Basis and Phenotype of Methicillin

Resistance in Staphylococcus aureus and Insights Into New β-lactams That Meet the Challenge, Antimicrob. Agents Chemother. 2009, 53, 4051-4063.

225. Zhang, W.; Fisher, J. F.; Mobashery, S. The Bifunctional Enzymes of Antibiotic

Resistance, Curr. Opin. Microbiol. 2009, 12, 505-511. 226. Chen, Y.; Zhang, W.; Shi, Q.; Hesek, D.; Lee, M.; Mobashery, S.; Shoichet, B. K. Crystal

Structures of Penicillin-Binding Protein 6 from Escherichia coli, J. Am. Chem. Soc. 2009, 131, 14345-14354.

227. Tao, P.; Fisher, J.; Shi, Q.; Vreven, T.; Mobashery, S.; Schlegel, H.B. Matrix

Metalloproteinase 2 (MMP2) Inhibition: QM/MM Studies of the Inhibition Mechanism of SB-3CT and its Analog, Biochemistry 2009, 48, 9839-9847.

228. Frase, H.; Shi, Q.; Testero, S. A.; Mobashery, S.; Vakulenko, S. B. Mechanistic Basis for

the Emergence of Catalytic Competence Against Carbapenem Antibiotics by the GES Family of β-Lactamases, J. Biol. Chem. 2009, 284, 29509-29513.

229. Forbes, C.; Shi, Q.; Fisher, J. F.; Lee, M.; Hesek, D.; Llarrull, L. I.; Toth, M.; Gossing, M.;

Fridman, R.; Mobashery, S. Active Site Ring-Opening of a Thiirane Moiety and Picomolar Inhibition of Gelatinases, Chem. Biol. Drug Design 2009, 79, 527-534.


22

230. Gooyit, M.; Lee, M.; Hesek, D.; Boggess, B.; Oliver, A. G.; Fridman, R.; Mobashery, S.; Chang, M. Synthesis, Kinetic Characterization and Metabolism of Diastereomeric 2-(1-(4-Phenoxyphenylsulfonyl)ethyl)thiiranes as Potent Gelatinase and MT1-MMP Inhibitors, Chem. Biol. Drug Design 2009, 79, 535-546.

231. Ota, R.; Kurihara, C.; Tsou, T.-L.; Young, W.; Yeghiazarians, Y.; Chang, M.; Mobashery,

S.; Sakamoto, A; Hashimoto, T. Roles of Matrix Metalloproteinases in Flow-Induced Outward Vascular Remodeling. J. Cereb. Blood Flow Metab. 2009, 29, 1547-1558.

232. Fisher, J. F.; Mobashery, S. Three Decades of the Class A β-Lactamase Acyl-Enzyme,

Curr. Protein Pept. Sci. 2010, 10, 401-407 (issue dedicated to the memory of Tony Fink). 233. Toth, M.; Smith, C.; Frase, H.; Mobashery, S. Vakulenko, S. An Antibiotic-Resistance

Enzyme from a Deep-Sea Bacterium, J. Am. Chem. Soc. 2010, 132, 816-823. 234. O'Daniel, P.; Zajicek, J.; Zhang, W.; Shi, Q.; Fisher, J.; Mobashery, S. Elucidation of the

Structure of the Membrane Anchor of Penicillin-Binding Protein 5 of Escherichia coli, J. Am. Chem. Soc. 2010, 132, 4110-4118.

235. Fernández, D.; Testero, S.; Vendrell, J.; Avilés, F. X.; Mobashery, S. The X-Ray Structure

of Carboxypeptidase A Inhibited by a Thiirane Mechanism-Based Inhibitor, Chem. Biol. Drug Design 2010, 75, 29-34.

236. Fisher, J. F. and Mobashery, S. “Mechanism-based Profiling of MMPs” in Methods Mol.

Biol. (Matrix Metalloproteinase Protocols), Vol. 622, Clark, I.M., Ed., Humana Press, 2010; pp. 471–487.

237. Tao, P.; Fisher, J. F.; Shi, Q.; Mobashery, S.; Schlegel, H. B. Matrix Metalloproteinase 2

(MMP2) Inhibition: DFT and QM/MM Studies of the Deprotonation Initiated Ring Opening Reaction of Sulfoxide Analog of SB-3CT, J. Phys. Chem. 2010, 114, 1030-1037.

238. Fisher, J. F.; Mobashery, S. Enzymology of Antibacterial Resistance, In Comprehensive

Natural Products Chemistry II, Chemistry and Biology, Mander, L., Liu, H. W. (Eds.), Elsevier: Oxford, 2010, pp443-487.

239. Pérez-Dorado, I. González, A.; Morales, M.; Sanles, R.; Striker, W.; Vollmer, W.;

Mobashery, S.; García, J. L.; Martínez-Ripoll, M.; García, P.; Hermoso, J. A. Insights into pneumococcal fratricide from crystal structure of the modular killing factor LytC, Nat. Struc. Mol. Biol. 2010, 17, 576-582.

240. Yamaguchi, T.; Hesek, D.; Lee, M.; Oliver, A. G.; Mobashery, S. Sulfonylation-Induced N-

to O-Acetyl Migration in 2-Acetamidoethanol Derivatives, J. Org. Chem. 2010, 75, 3515-3517.

241. Testero, S. A.; Fisher, J. F.; Mobashery, S. β-Lactam Antibiotics in Burger's Medicinal

Chemistry, Drug Discovery and Development, Vol. 7 (Antiinfectives), Abraham, D. J. and Rotella, D. P. (Eds.), Wiley and Sons, 2010, pp259-404.

242. Fisher, J.; Mobashery, S. 2007 Astellas USA Foundation Award: Host-Guest Chemistry of

the Peptidoglycan, J. Med. Chem. 2010, 53, 4813-4829. PMID:20524613 243. Bernal, P.; Lemaire, S.; Pinho, M. G.; Mobashery, S.; Hinds, J.; Taylor, P.W. Insertion of

Epicatechin Gallate into the Cytoplasmic Membrane of Methicillin-Resistant


23

Staphylococcus Aureus Disrupts Penicillin-Binding Protein (PBP) 2a-Mediated β-Lactam Resistance by Delocalizing PBP2, J. Biol. Chem. 2010, 285, 24055-24065.

244. Llarrull, L.; Prorok, M.; Mobashery, S. Binding of the Gene Repressor BlaI to the bla

Operon in Methicillin-Resistant Staphylococcus aureus, Biochemistry 2010, 49, 7975-7977.

245. Llarrull, L. I.; Testero, S. A.; Fisher, J. F.; Mobashery, S. The Future of the β-Lactams,

Curr. Opin. Microbiol. 2010, 13, 551-557. PMID:20888287 246. Zhou, J.; Tao, P.; Fisher, J. F.; Shi, Q.; Mobashery, S.; Schlegel, H. B. QM/MM Studies of

the Matrix Metalloproteinase 2 (MMP2) Inhibition Mechanism of (S)-SB-3CT and its Oxirane Analogue, J. Chem. Theo. Comp. 2010, 6, 3580-3587.

247. Lee, M.; Hesek, D.; Shah, I. M., Oliver, A. G.; Dworkin, J.; Mobashery, S. Synthetic

Peptidoglycan Motifs for Germination of Bacterial Spores, ChemBioChem 2010, 11, 2525-2529. PMID:21117117

248. Artola-Recolons, C.; Llarrull, L. I.; Lastochkin, E.; Mobashery, S.; Hermoso, J. A.

Crystallization and Preliminary X-Ray Diffraction Analysis of Lytic Transglycosylase MltE from Escherichia coli, Acta Crystal. F. 2011, F67, 161-163.

249. Testero, S. A.; Lee, M.; Staran, R.; Espahbodi, M.; Llarrull, L.; Toth, M.; Mobashery, S.;

Chang, M. Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors, ACS Med. Chem. Lett. 2011, 2, 177-181.

250. Testero, S. A.; Llarrull, L. I.; Fisher, J. F.; Chang, M.; Mobashery, S. Exploring the

Functional Space of Thiirane as Gelatinase Inhibitors Using Click Chemistry, Arkivoc 2011, vii, 221-236.

251. Chongsiriwantan, N. P.; Miller, T. M.; Wetzler, M.; Vakulenko, S.; Karlsson, A. J.;

Palacek, S. P.; Mobashery, S.; Barron, A. E. Short Alkylated Peptoid Mimetics of Antimicrobial Lipopeptides, Antimicrob. Agents Chemother. 2011, 55, 417-420.

252. Maestro, B.; Nováková, L.; Hesek, D.; Lee, M.; Leyva, E.; Mobashery, S.; Sanz, J. M.;

Branny, P. Recognition of Peptidoglycan and β-Lactam Antibiotics by the Extracellular Domain of the Ser/Thr Protein Kinase StkP from Streptococcus pneumoniae, FEBS Lett. 2011, 585, 357-363.

253. Shi, Q.; Meroueh, S.; Fisher, J.; Mobashery, S. A. Computational Evaluation of the

Mechanism of Penicillin-Binding Protein Catalyzed Cross-linking of the Bacterial Cell Wall, J. Am. Chem. Soc. 2011, 133, 5274-5283.

254. Artola-Recolons, C.; Carrasco-López, C.; Llarrull, L.; Kumarasiri, M.; Lastochkin, E.;

Martínez de Ilarduya, I.; Meindl, K.; Usón, I.; Mobashery, S.; Hermoso, J. High-Resolution Crystal Structure of an Outer Membrane-Anchored Endolytic Peptidoglycan Lytic Transglycosylase (MltE) from Escherichia coli, Biochemistry 2011, 50, 2384-2386.

255. Frase, H.; Smith, C. A.; Toth, M.; Champion, M. M.; Mobashery, S.; Vakulenko, S. B.

Identification of Products of Inhibition of GES-2 β-Lactamase by Tazobactam by X-ray Crystallography and Spectrometry, J. Biol. Chem. 2011, 286, 14396-14409.


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256. Testero, S. A.; Bouley, R.; Fisher, J. F.; Chang, M.; Mobashery, S. Exploration of Mild Copper-Mediated Coupling of Organotrifluoroborates in the Synthesis of Thiirane-Based Inhibitors of Matrix Metalloproteinases, Bioorg. Med. Chem. Lett. 2011, 21, 2675-2678.

257. Benson, H. L.; Mobashery, S.; Chang, M.; Kheradmand, F.; Hong, J. S.; Smith, G. N.;

Shilling, R. A.; Wilkes, D. S. Endogenous MMP2 and MMP9 Regulate Activation of CD4+ and CD8+ T cells, Am. J. Resp. Cell Mol. Biol., 2011, 44, 700-708.

258. Antunes, N. T.; Frase, H.; Toth, M.; Mobashery, S.; Vakulenko, S. B. Resistance to the

Third-Generation Cephalosporin Ceftazidime by a Deacylation-Deficient Mutant of the TEM β-Lactamase by the Uncommon Covalent-Trapping Mechanism, Biochemistry 2011, 50, 6387-6395.

259. Borbulevych, O.; Kumarasiri, M.; Wilson, B.; Llarrull, L. I.; Lee, M.; Hesek, D.; Shi, Q.;

Peng, J.; Baker, B. M.; Mobashery, S. Lysine Nζ-Decarboxylation Switch and Activation of the β-Lactam-Sensor Domain of BlaR1 of Methicillin-Resistant Staphylococcus aureus, J. Biol. Chem. 2011, 286, 31466-31472.

260. Carrasco-López,C.; Rojas-Altuve, A.; Zhang, W.; Hesek, D.; Lee, M.; Barbe, S.; André, I.;

Ferrer, P.; Silva-Martin, N.; Castro, G.R. Martínez-Ripoll, M.; Mobashery, S. Hermoso, J. A., Crystal Structures of Bacterial Peptidoglycan Amidase AmpD and an Unprecedented Activation Mechanism, J. Biol. Chem. 2011, 286, 31714-31722.

261. Sohail, A.; Marco, M.; Zhao, H.; Shi, Q.; Merriman, S.; Mobashery, S.; Fridman, R.

Characterization of the Dimerization Interface of Membrane Type 4 (MT4)-Matrix Metalloproteinase (MMP), J. Biol. Chem. 2011, 286, 33178-33189.

262. Gooyit, M.; Lee, M.; Schroeder, V.; Ikejiri, M.; Suckow, M.; Mobashery, S.; Chang, M.

Selective Water-Soluble Gelatinase Inhibitor Prodrugs, J. Med. Chem. 2011, 54, 6676-6690.

263. Llarrull, L. I.; Toth, M.; Champion, M. M.; Mobashery, S. Activation of BlaR1 Protein of

Methicillin-Resistant Staphylococcus aureus, Its Proteolytic Processing and Recovery from Induction of Resistance, J. Biol. Chem. 2011, 286, 38148-38158.

264. Bush, K.; Courvalin, P.; Dantas, G.; Davies, J.; Eisenstein, B.; Huovinen, P.; Jacoby, G. A.;

Kishony, R.; Kreiswirth, B. N.; Kutter, E.; Lerner, S. A.; Levy, S.; Lewis, K.; Lomovskaya, O.; Miller, J. H.; Mobashery, S.; Piddock, L. J. V.; Projan, S.; Thomas, C. M.; Tomasz, A.; Tulkens, P. M.; Walsh, T. R.; Watson, J. D.; Witkowski, J.; Witte, W.; Wright, G.; Yeh, P.; Zgurskaya, H. I. Tackling Antibiotic Resistance, Nat. Rev. Microbiol. 2011, 9, 894-896.

265. Park, J. S.; Lee, W. C.; Yeo, K. J.; Ryu, K. S.; Kumarasiri, M.; Hesek, D.; Lee, M.;

Mobashery, S.; Song, J. H.; Kim, S. I.; Lee, J. C.; Cheong, C.; Jeon, Y. H.; Kim, H. Y. Mechanism of Anchoring of OmpA Protein to the Cell-Wall Peptidoglycan of the Gram-Negative Bacterial Outer Membrane JASEB J. 2012, 26, 219-228.

266. Kumarasiri, M.; Llarrull, L. I.; Borbulevych, O.; Fishovitz, J.; Lastochkin, E.; Baker, B.

M.; Mobashery, S. An Amino-Acid Position at the Crossroads of Evolution of Protein Function: Antibiotic-Sensor Domain of the BlaR1 Protein from Staphylococcus aureus vs. Class D β-Lactamases, J. Biol. Chem. 2012, 287, 8232-8241.

267. Yamaguchi, T.; Blázquez, B.; Hesek, D.; Lee, M.; Llarrull, L.; Boggess, B.; Oliver, A.;

Fisher, J.; Mobashery, S. Inhibitors for Bacterial Cell-Wall Recycling, ACS Med. Chem. Lett. 2012, 3, 238-242.


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268. Boudreau, M. A.; Fisher, J. F.; Mobashery, S. Messenger Functions of the Bacterial Cell

Wall-derived Muropeptides, Biochemistry 2012, 51, 2974-2990. 269. Llarrull, L. I.; Mobashery, S. Dissection of Events in Resistance to β-Lactam Antibiotics

Mediated by the Protein BlaR1 from Staphylococcus aureus, Biochemistry 2012, 51, 4642-4649.

270. Lee, M.; Ikejiri, M.; Klimpel, D.; Toth, M.; Espahbodi, M.; Hesek, D.; Forbes, C.;

Kumarasiri, M.; Noll, B.; Chang, M.; Mobashery, S. Structure-Activity Relationship for Thiirane-Based Gelatinase Inhibitors, ACS Med. Chem. Lett. 2012, 3, 490-495.

271. Gooyit, M; Suckow, M.; Schroeder, V.; Wolten, W.; Mobashery, S.; Chang, M. Selective

Gelatinase Inhibitor Neuroprotective Agents Cross the Blood-Brain Barrier, ACS Chem. Neurosci. 2012, 3, 730-736.

272. Mazel, D.; Mobashery, S. Antibiotics as Physiological Stress Inducers and Bacterial

Response to the Challenge, Curr. Opin. Microbiol 2012, 15, 553-554. 273. Makino, H.; Tada, Y.; Wada, K.; Liang, E. I.; Chang, M.; Mobashery, S.; Kanematsu, Y.;

Kurihara, C.; Kanematsu, M.; Kitazato, K.; Hashimoto, T. Pharmacological Stabilization of Intracranial Aneurysms in Mice―A Feasibility Study, Stroke 2012, 43, 2450-2456.

274. Cui, J.; Chen, S.; Zhang, C.; Meng, F.; Wu, W.; Hu, R.; Or, H.; Lehmidi, T.; Blair, G. J.;

Lee, M.; Chang, M.; Mobashery, S.; Sun, G. Y., Gu, Z. Inhibition of MMP-9 by a Selective Gelatinase Inhibitor Protects Neurovasculature from Embolic Focal Cerebral Ischemia, Molec. Neurodegeneration 2012, 7, 21.

275. Hesek, D.; Lee, M.; Zajicek, J.; Fisher, J.; Mobashery, S. Synthesis and NMR

Characterization of Z,Z,Z,Z,E,E,ω-Heptaprenol, J. Am. Chem. Soc. 2012, 134, 13881-13888.

276. Smith, C. A.; Frase, H.; Toth, M.; Kumarasiri, M.; Wiafe, K.; Munoz, J.; Mobashery, S.;

Vakulenko, S. B. Structural Basis for Progression Toward the Carbapenemase Activity in the GES Family of β-Lactamases, J. Am. Chem. Soc. 2012, 134, 19512-19515.

277. Lee, M.; Hesek, D.; Llarrull, L. I.; Lastochkin, E.; Pi, H.; Boggess, B.; Mobashery, S.

Reactions of All Escherichia coli Lytic Transglycosylases with Bacterial Cell Wall, J. Am. Chem. Soc. 2013, 135, 3311-3314.

278. Zhang, W.; Lee, M.; Hesek, D.; Lastochkin, E.; Boggess, B.; Mobashery, S. Reactions of

the Three AmpD Enzymes of Pseudomonas aeruginosa, J. Am. Chem. Soc. 2013, 135, 4950-4953.

279. Martínez-Caballero, S.; Lee, M.; Artola-Recolons, C.; Carrasco-López, C.; Hesek, D.;

Spink, E.; Lastochkin, E.; Zhang, W.; Hellman, L.; Boggess, B.; Mobashery, S.; Hermoso, J. Reaction Products and X-Ray Structure of AmpDh2, a Virulence Determinant of Pseudomonas aeruginosa, J. Am. Chem. Soc. 2013, 135, 10318-10321.

280. Lee, M.; Artola-Recolons, C.; Carrasco-López, C.; Martínez-Caballero, S.; Hesek, D.;

Spink, E.; Lastochkin, E.; Zhang, W.; Hellman, L.; Boggess, B.; Hermoso, J.; Mobashery,


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S. Cell-Wall Remodeling by the Zinc-Protease AmpDh3 from Pseudomonas aeruginosa J. Am. Chem. Soc. 2013, 135, 12604-12607.

281. Johnson, J. J.; Fisher, J. F.; Mobashery, S. Bacterial Cell-Wall Recycling, Ann. NY Acad.

Sci. 2013, 1277, 54-75. 282. Kumarasiri, M.; Fisher, J. F.; Mobashery, S. Penicillin-Binding Protein 5 of Escherichia

coli, in Handbook of Proteolytic Enzymes, Neil D. Rawlings and Guy S. Salvesen, Editors, Third Edition, Elsevier Press, Oxford, UK, 2013, 3474-3480.

283. Fu, H. L.; Valiathan, R. R.; Arkwright, R.; Sohail, A.; Mihai, C.; Kumarasiri, M.;

Mahasenan, K.; Mobashery, S.; Huang, P.; Agarwal, G.; Fridman, R. Discoidin Domain Receptors: Unique Receptor Tyrosine Kinases in Colalgen-Mediated Signaling, J. Biol. Chem. 2013, 288, 7430-7437.

284. Fu, H. L.; Sohail, A.; Valiathan, R. R.; Wasinski, B. D.; Kumarasiri, M.; Mahasenan, K. V.; Bernardo, M. M.; Tokmina-Roszyk, D.; Fields, G. B.; Mobashery, S.; Fridman, R. Shedding of Discoidin Domain Receptor (DDR) 1 by Membrane-Type (MT)-Matrix Metalloproteinases (MMPs), J. Biol. Chem. 2013, 288, 12114-12129.

285. Smith, J.; Kumarasiri, M.; Zhang, W.; Hesek, D.; Lee, M.; Toth, M.; Vakulenko, S.; Fisher,

J. F.; Mobashery, S.; Chen, Y. A Structural Analysis of the Role of the Pseudomonas aeruginosa Penicillin-Binding Protein 5 in β-Lactam Resistance, Antimicrob. Agents Chemother. 2013, 57, 3137-3146.

286. Otero, L.H.; Rojas-Altuve, A.; Llarrull, L.I.; Carrasco-López, C.; Kumarasiri, M.;

Lastochkin, E., Fishovitz, J.; Dawley, M.; Hesek, D.; Lee, M.; Johnson, J.W.; Fisher, J.F.; Chang, M.; Mobashery, S.; Hermoso, J.A. How Allosteric Control of Staphylococcus aureus Penicillin-Binding Protein 2a Enables Methicillin-Resistance and Physiological Function, Proc. Natl. Acad. Sci. USA, 2013, 110, 16808-16813.

287. Hadass, O.; Tomlison, B. N.; Gooyit, M.; Chen, S.; Purdy, J. J.; Walker, J. M.; Zhang, C.;

Giritharan, A. B.; Purnell, W.; Robinson, C. R. II; Shin, D.; Schroeder, V. A.; Suckow, M. A.; Simonyi, A.; Sun, G. Y.; Mobashery, S.; Cui, J.; Chang, M.; Gu, Z. Selective Inhibition of Matrix Metalloproteinase-9 Attenuates Secondary Damage Resulting from Severe Traumatic Brain Injury, PLoS One 2013, 8, e76904.

288. Gooyit, M.; Song, W.; Mahasenan, K.; Lichtenwalter, K.; Suckow, M.; Schroeder, V.; Wolter, W.; Mobashery, S.; Chang, M. Phenyl Carbamate and Phenyl Urea Thiiranes as Selective Matrix Metalloproteinase-2 Inhibitors that Cross the Blood-Brain Barrier, J. Med. Chem. 2013, 56, 8139-8150.

289. Smith, C. A.; Antunes, N. T.; Stewart, N. K.; Toth, M.; Kumarasiri, M.; Chang, M.;

Mobashery, S.; Vakulenko, S. B. Structural Basis for Carbapenemase Activity of the OXA-23 β-Lactamase from Acinetobacter baumannii, Chem. & Biol. 2013, 20, 1107-1115.

290. Jedinak, L.; Rush, L.; Lee, M.; Hesek, D.; Fisher, J.; Boggess, B.; Noll, B.; Mobashery, S.

Use of Silver Carbonate in the Witting Reaction, J. Org. Chem. 2013, 78, 12224-12228. 291. Leemans, E.; Fisher, J. F.; Mobashery, S. The β-Lactam Antibiotics: Their Future in the

Face of Resistance, in Antimicrobials: Novel and Old Molecules in the Fight Against Multi-resistant Bacteria, Flavia Marinelli and Olga Genilloud (Eds.) Springer Verlag, 2014, pp59-85.


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292. Gooyit, M.; Peng, Z.; Wolter, W.; Pi, H.; Ding, D.; Hesek, D.; Lee, M.; Boggess, B.; Champion, M.; Suckow, M.; Mobashery, S.; Chang, M. A Chemical Biological Strategy to Facilitate Diabetic Wound Healing, ACS Chem. Biol. 2014, 9, 505-510.

293. Frederick, T. E.; Wilson, B. D.; Cha, J.; Mobashery, S.; Peng, J. W. Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy, Biochemistry 2014, 53, 10-12.

294. Blázquez, B.; Llarrull, L.; Luque-Ortega, J.; Alfonso, C.; Boggess, B.; Mobashery, S.

Regulation of Expression of the β-Lactam Antibiotic-Resistance Determinants in Methicillin-Resistant Staphylococcus aureus (MRSA), Biochemistry 2014, 53, 1548-1550.

295. Fu, H. L.; Valiathan, R. R.; Payne, L.; Kumarasiri, M.; Mahasenan, K. V.; Mobashery, S.;

Huang, P.; Fridman, R. Glycosylation at Asn211 Regulates the Activation State of the Discoidin Domain Receptor 1 (DDR1), J. Biol. Chem. 2014, 289, 9275-9287.

296. O'Daniel, P. I.; Peng, Z.; Pi, H.; Testero, S. A.; Ding, D.; Spink, E.; Leemans, E.; Boudreau,

M. A.; Yamaguchi, T.; Schroeder, V. A.; Wolter, W. R.; Llarrull, L. I.; Song, W.; Lastochkin, E.; Kumarasiri, M.; Antunes, N. T.; Espahbodi, M.; Lichtenwalter, K.; Suckow, M. A.; Vakulenko, S.; Mobashery, S.; Chang, M. Discovery of a New Class of Non-β-Lactam Inhibitors of Penicillin-Binding Proteins with Gram-Positive Antibacterial Activity, J. Am. Chem. Soc. 2014, 136, 3664-3672.

297. Fishovitz, J.; Rojas-Altuve, A.; Otero, L.; Dawley, M.; Carrasco-López, C.; Chang, M.;

Hermoso, J.; Mobashery, S. Disruption of Allosteric Response as an Unprecedented Mechanism of Resistance to Antibiotics, J. Am. Chem. Soc. 2014, 136, 9814-9817.

298. Mellroth, P.; Sandalova, T.; Kikhney, A.; Vilaplana, F.; Hesek, D.; Lee, M.; Mobashery, S.;

Normark, S.; Svergun, D.; Henriques-Normark, B.; Achour, A. Structural and Functional Insights into Peptidoglycan Access for the Lytic Amidase LytA of Streptococcus pneumoniae, mBio 2014, 5, e01120-13.

299. Kumarasiri, M.; Zhang, W.; Shi, Q.; Fisher, J. F.; Mobashery, S. Protonation States of

Active-Site Lysines of Penicillin-Binding Protein 6 from Escherichia coli and the Mechanistic Implications, PROTEINS: Structure, Function, and Bioinformatics 2014, 82, 1348-1358.

300. Fisher, J. F.; Mobashery, S. The Sentinel Role of Peptidoglycan Recycling in the β-Lactam

Resistance of the Gram-Negative Enterobacteriaceae and Pseudomonas aeruginosa, Bioorg. Chem. 2014, 56, 41-48.

301. Ding, D.; Lichtenwalter, K.; Pi, H.; Mobashery, S.; Chang, M. Characterization of a

Aelective Inhibitor for Matrix Metalloproteinase-8 (MMP-8), Med. Chem. Comm. 2014, 5, 1381-1383.

302. Xiao, Q.; Vakulenko, S.; Chang, M.; Mobashery, S. Mutations in mmpL and in Cell-Wall

Stress Stimulon Contribute to Resistance to Oxadiazole Antibiotics in Methicillin-Resistant Staphylococcus aureus, Antimicrob. Agents Chemother. 2014, 58, 5841-5847.

303. Artola-Recolons, C.; Lee, M.; Bernardo-García, N.; Blázquez, B.; Hesek, D.; Bartual, S. G.;

Mahasenan, K.; Lastochkin, E.; Pi, H.; Boggess, B.; Meindl, K.; Usón, I.; Fisher, J. F.; Mobashery, S.; Hermoso, J. A. Structure and Cell Wall Cleavage by Modular Lytic Transglycosylase MltC of Escherichia coli, ACS Chem. Biol. 2014, 9, 2058-2066.


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304. Fishovitz, J.; Hermoso, J.; Chang, M.; Mobashery, S. Penicillin-Binding Protein 2a of Methicillin-Resistant Staphylococcus aureus, Int. Union Biochem. Molec. Biol. Life. 2014, 66, 572-577.

305. Kim, H. S.; Kim, J.; Im, H. N.; An, D. R.; Lee, M.; Hesek, D.; Mobashery, S.; Kim, J. Y.;

Cho, K.; Yoon, H. J.; Han, B. W.; Lee. B. I.; Suh, S. W. Structural Basis for the Recognition of Muramyltripeptide by Helicobacter pylori Csd4, a D,L-carboxypeptidase controlling the helical cell shape, Acta Crystal. 2014, D70, 2800-2812.

306. Lee, M.; Hesek, D.; Noll, B. C.; Oliver, A. G.; Mobashery, S. Structures of (R) and (S)-2-(4-

Phenoxyphenylsulfonylmethyl)thiirane, Acta Crystal. 2014, C70, 1003-1006. 307. Fisher, J. F.; Johnson, J. W.; Mobashery, S. Strategies for circumventing bacterial resistance

mechanisms. In Handbook of Antimicrobial Resistance; Götte, M., Berghuis, A., Matlashewski, G., Wainberg, M., Sheppard, D., Eds.; Springer Science+Business Media: New York, 2017; pp 231–261.

308. Lee, M.; Hesek, D.; Blázquez, B.; Lastochkin, E.; Boggess, B.; Fisher, J.; Mobashery, S.

Catalytic Spectrum of the Penicillin-Binding Protein 4 of Pseudomonas aeruginosa, a Nexus for the Induction of β-Lactam Antibiotic Resistance, J. Am. Chem. Soc. 2015, 137, 190-200.

309. Bouley, R.; Kumarasiri, M.; Peng, Z.; Otero, L.; Song, W.; Suckow, M.; Schroeder, V.;

Wolter, W.; Lastochkin, E.; Antunes, N.; Pi, H.; Vakulenko, S.; Hermoso, J.; Chang, M.; Mobashery, S. Discovery of Antibiotic (E)-3-(3-Carboxyphenyl)-2-(4-cyanostyryl)quinazolin-4(3H)-one, J. Am. Chem. Soc. 2015, 137, 1738-1741.

310. Fishovitz, J.; Taghizadeh, N.; Fisher, J.; Chang, M.; Mobashery, S. The Tipper-Strominger

Hypothesis and Triggering of Allostery in Penicillin-Binding Protein 2a of Methicillin-Resistant Staphylococcus aureus (MRSA), J. Am. Chem. Soc. 2015, 137, 6500-6505.

311. An, D. R.; Kim, H. S.; Kim, J.; Im, H. N.; Yoon, H. J.; Yoon, J. Y.; Jang, J. Y.; Hesek, D.;

Lee, M.; Mobashery, S.; Kim, S. J.; Lee, B. I.; Suh, S. W. Crystal Structure of Csd3 from Helicobacter pylori, a Cell-Shape Determining Metallopeptidase, Acta Crystal. 2015, D71, 675-686.

312. Spink, E.; Ding, D.; Peng, Z.; Boudreau, M.; Leemans, E.; Lastochkin, E.; Song, W.;

Lichtenwalter, K.; O'Daniel, P.; Testero, S.; Pi, H.; Schroeder, V.; Wolter, W.; Antunes, N.; Suckow, M.; Vakulenko, S.; Chang, M.; Mobashery, S. Structure-Activity Relationship for the Oxadiazole Class of Antibiotics, J. Med. Chem. 2015, 58, 1380-1389.

313. Staude, M. W.; Frederick, T. E.; Natarajan, S. V.; Wilson, B. D.; Tanner, C. E.; Rugiero, S.

T.; Mobashery, S.; Peng, J. W. Investigation of Signal Transduction Routes within the Sensor/Transducer Protein BlaR1 of Staphylococcus aureus, Biochemistry 2015, 54, 1600-1610.

314. Acebrón, I.; Chang, M.; Mobashery, S.; Hermoso, J. A. The Allosteric Site for the Nascent

Cell Wall in Penicillin-Binding Protein 2a: an Achilles’ Heel of Methicillin-Resistant Staphylococcus aureus, Curr. Med. Chem. 2015, 22, 1678-1686.

315. Wang, H.; Lee, M.; Peng, Z.; Blázquez, B.; Lastochkin, E.; Kumarasiri, M.; Bouley, R.;

Chang, M.; Mobashery, S. Synthesis and Evaluation of 1,2,4-Triazolo[1,5-a]pyrimidines as Antibacterial Agents Against Enterococcus faecium, J. Med. Chem. 2015, 58, 4194-4203.


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316. Fisher, J. F.; Mobashery, S. Bacterial Cell Wall: Morphology and Biochemistry, in Practical Handbook of Microbiology, Third Edition (Goldman, E., and Green, L. H., Eds.), 2015, pp. 221–264, CRC Press (Taylor & Francis Group), Boca Raton, FL.

317. Turapov, O.; Loraine, J.; Jenkins, C. H.; Barthe, P.; McFeely, D.; Forti, F.; Ghisotti, D.;

Hesek, D.; Lee, M.; Bottrill, A. R.; Vollmer, W.; Mobashery, S.; Cohen-Gonsaud, M.; Mukamolova, G. V. The External PASTA Domain of the Essential Serine/Threonine Protein Kinase PknB Regulates Mycobacterial Growth, Open Biol. 2015, 5, 150025.

318. Lee, M.; Rucil. T.; Hesek, D.; Oliver, A. G.; Fisher, J. F.; Mobashery, S. Regioselective

Control of the SNAr Amination of 5-Substituted-2,4-Dichloropyrimidines Using Tertiary Amine Nucleophiles, J. Org. Chem. 2015, 80, 7757-7763.

319. Galimand, M.; Fishovitz, J.; Lambert, T.; Barbe, V.; Zajíček, J.; Mobashery, S.; Courvalin,

P. AAC(3)-XI, a New Aminoglycoside 3-N-Acetyltransferase from Corynebacterium striatum, Antimicrob. Agents Chemother. 2015, 59, 5647-5653.

320. Gonzales, P. R.; Pesesky, M.; Bouley, R.; Ballard, A.; Biddy, B. A.; Suckow, M. A.;

Wolten, W. R.; Schroeder, V. A.; Burnham, C. D.; Mobashery, S.; Chang, M.; Dantas, G. Synergistic, Collaterally Sensitive β-Lactam Combinations Suppress Resistance in MRSA, Nat. Chem. Biol. 2015, 11, 855-861.

321. Ding, D.; Boudreau, M. A.; Leemans, E.; Spink, E.; Yamaguchi, T.; Testero, S. A.;

O’Daniel, P. I.; Lastochkin, E.; Chang, M.; Mobashery, M. Exploration of the Structure-Activity Relationship of 1,2,4-Oxadiazole Antibiotics, Bioorg. Med. Chem. Lett. 2015, 25, 4854-4857.

322. Kim, H. S.; Im, H. N.; An, D. R.; Yoon, J. Y.; Jang, J. Y.; Mobashery, S.; Hesek, D.; Lee,

M.; Yoo, J.; Cui, M.; Choi, S.; Kim, C.; Lee, N. K.; Kim, S. J.; Kim, J. Y.; Bang, G.; Han, B. W.; Lee, B. I.; Yoon, H. J.; Suh, S. W. The Cell-Shape Determining Csd6 Protein from Helicobacter pylori Constitutes a New Family of L,D-carboxypeptidase, J. Biol. Chem. 2015, 290, 25103-25117.

323. Boudreau, M.; Fishovitz, J.; Llarrull, L.; Xiao, Q.; Mobashery, S. Phosphorylation of BlaR1

in Manifestation of Antibiotic Resistance in Methicillin-Resistance Staphylococcus aureus and its Abrogation by Small Molecules, ACS Infect. Dis. 2015, 1, 454-459.

324. Gao, M.; Nguyen, T. T.; Suckow, M. A.; Wolten, W. R.; Gooyit, M.; Mobashery, S.; Chang,

M. Acceleration of Diabetic Wound Healing Using a Novel Protease-Anti-Protease Combination Therapy, Proc. Natl. Acad. Sci. U. S. A. 2015, 112, 15226-152231.

325. Lee, M.; Chen, Z.; Tomlinson, B.; Gooyit, M.; Hesek, D.; Juarez, M.; Nizam, R.; Boggess,

B.; Lastochkin, E.; Schroeder, V.; Wolter, W.; Suckow, M.; Cui, J.; Mobashery, S.; Gu, Z.; Chang, M. Water-Soluble MMP-9 Inhibitor Reduces Lesion Volume After Severe Traumatic Brain Injury, ACS Chem. Neurosci. 2015, 6, 1658-1664.

326. Rico-Lastres, P; Díez-Martínez, R.; Iglesias-Bexiga, M; Bustamante, N; Aldridge, C.;

Hesek, D.; Lee, M.; Mobashery, S.; Gray, J.; Vollmer, W.; García, P.; Menéndez, M. Substrate recognition and catalysis by LytB, a pneumococcal peptidoglycan hydrolase involved in virulence, Scientific Reports 2015, 5, 16198.

327. Fisher, J. F.; Mobashery, S. The β-Lactam (Azetidin-2-one) as a Privileged Ring in

Medicinal Chemistry, Privileged Scaffolds in Medicinal Chemistry, Bräse, S. (Ed.), Royal Society of Chemistry Publishing, 2016, 64-97.


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328. Gooyit, M; Peng, Z.; Mobashery, S.; Chang, M. Thiirane Class of Gelatinase Inhibitors as a

Privileged Template that Crosses the Blood-Brain Barrier, Privileged Scaffolds in Medicinal Chemistry, Bräse, S. (Ed.), Royal Society of Chemistry Publishing, 2016, 262-286.

329. Fisher, J. F.; Mobashery, S. Endless Resistance. Endless Antibiotics? MedChemComm.

2016, 7, 37-49. 330. Leemans, E.; Mahasenan, K. V.; Kumarasiri, M.; Spink, E.; Ding, D.; O’Daniel, P.;

Boudreau, M. A.; Lastochkin, E.; Testero, S. A.; Yamaguchi, T.; Lee, M.; Hesek, D.; Fisher, J. F.; Chang, M.; Mobashery, S. Three-Dimensional QSAR Analysis and Design of New 1,2,4-oxadiazoles Antibacterials, Bioorg. Med. Chem. Lett. 2016, 26, 1011-1015.

331. Wang, H.; Hesek, D.; Lee, M.; Lastochkin, E.; Oliver, A.; Chang, M.; Mobashery, S. The

Natural Product Essramycin and Three of Its Isomers Are Devoid of Antibacterial Activity, J. Nat. Prod. 2016, 79, 1219-1222.

332. Fisher, J. F.; Mobashery, S. β-Lactam Resistance Mechanisms: Gram-Positive Bacteria

and Mycobacterium tuberculosis. Cold Spring Harb Perspect Med 2016, 6, 45-63. 333. Lenz, J. D.; Stoh l, E. A.; Robertson, R.; Hackett, K. T.; Fisher, K; Xiong, K.; Lee, M.;

Hesek, D.; Mobashery, S.; Seifert, H. S.; Davies, C.; Dillard, J. P. Amidase activity of AmiC controls cell separation, stem-peptide release, and is enhanced by NlpD in Neisseria gonorrhoeae J. Biol. Chem. 2016, 291, 10916-10933.

334. Bouley, R.; Ding, D.; Peng, Z.; Bastian, M.; Lastochkin, E.; Song, W.; Suckow, M. A.;

Schroeder, V. A.; Wolter, W. R.; Mobashery, S.; Chang, M. Structure-Activity Relationship for the 4(3H)-Quinazolinone Antibacterials. J. Med. Chem. 2016, 69, 5011-5021.

335. Lee, M.; Dhar, S.; De Benedetti, S.; Hesek, D.; Boggess, B.; Blázquez, B.; Mathee, K.;

Mobashery, S. Muropeptide Pool and the Elicitors of β-Lactam-Antibiotic Resistance in Pseudomonas aeruginosa, Angew. Chem. Int. Ed. 2016, 55, 6862–6866.

336. Lee, M.; Domínguez-Gil, T.; Hesek, D.; Mahasenan, K. V.; Lastochkin, E.; Hermoso, J. A.;

Mobashery, S. Turnover of Bacterial Cell Wall by SltB3, a Multidomain Lytic Transglycosylase of Pseudomonas aeruginosa, ACS Chem. Biol. 2016, 11, 1525-1531.

337. Janardhanan, J.; Meisel, J. E.; Ding, D.; Schroeder, V. A.; Wolter, W. R.; Mobashery, S.;

Chang, M. In Vitro and In Vivo Synergy of the Oxadiazole Class of Antibacterials with β-Lactams. Antimicrob. Agents Chemother. 2016, 60, 5581-5588.

338. Sandalova T.; Lee M.; Henriques-Normark B.; Hesek D.; Mobashery S.; Mellroth P.;

Achour, A. The Crystal Structure of the Major Pneumococcal Autolysin LytA in Complex with a Large Peptidoglycan Fragment Reveals the Pivotal Role of Glycan for Lytic Activity, Mol. Microbiol. 2016, 101, 954-967.

339. Domínguez-Gil, T.; Lee, M.; Acebrón-Avalos, I; Mahasenan, K. V.; Hesek, D.; Dik, D.;

Byun, B. J.; Lastochkin, E.; Fisher, J. F.; Mobashery, S.; Hermoso, J. A. Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa, Structure 2016, 24, 1729-1741.

340. Nguyen, T. T.; Mobashery, S.; Chang, M. Roles of Matrix Metalloproteinases in Cutaneous

Wound Healing. In "Wound Healing: New Insights into Ancient Challenges". Alexandrescu, V. A. (Editor), 2016, Chapter 3, p. 37-71. ISBN 978-953-51-


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2679-9. 341. An, D. R.; Im, H. N.; Jang, J. Y.; Kim, H. S.; Kim, J.; Yoon, H. J.; Hesek, D.; Lee, M.;

Mobashery, S.; Kim, S. J.; Suh, S. W. Structural Basis of the Heterodimer Formation between Cell Shape-Determining Proteins Csd1 and Csd2 from Helicobacter pylori, PLOS One 2016, 11, e0164243.

342. Rivera, I.; Molina, R.; Lee, M.; Mobashery, S.; Hermoso, S. Orthologous and Paralogous

AmpD Peptidoglycan Amidases from Gram-Negative Bacteria, Microb. Drug Res. 2016, 22, 470–476.

343. Janardhanan, J.; Chang, M.; Mobashery, S. The Oxadiazole Antibacterials, Curr. Opin.

Microbiol. 2016, 33, 13–17. 344. Gao, M.; Zhang, H.; Trivedi, A.; Mahasenan, K.; Schroeder, V.; Wolter, W.; Suckow, M.;

Mobashery, S.; Noble-Haeusslein, L.; Chang, M. Selective Inhibition of MMP-2 Does Not Alter Neurological Recovery after Spinal Cord Injury, ACS Chem. Neurosci. 2016, 7, 1482-1487.

345. Schaub, R. E.; Chan, Y. A.; Lee, M.; Hesek, D.; Mobashery, S.; Dillard, J. P. Lytic

Transglycosylases LtgA and LtgD Facilitate Peptidoglycan Incorporation, Recycling, and Release of Peptidoglycan Monomers in Neisseria gonorrhoeae, Mol. Microbiol. 2016, 102, 865–881.

346. Dik, D. A.; Domínguez-Gil, T.; Lee, M.; Hesek, D.; Byun, B.; Fishovitz, J.; Boggess, B.;

Hellman, L. M.; Fisher, J. F.; Hermoso, J. A.; Mobashery, S. Muropeptide Binding and the X-Ray Structure of the Effector Domain of the Transcriptional Regulator AmpR of Pseudomonas aeruginosa, J. Am. Chem. Soc. 2017, 137, 1448–1451.

347. Mahasenan, K. V.; Molina, R.; Bouley, R.; Batuecas, M. T.; Fisher, J. F.; Hermoso, J. A.;

Chang, M.; Mobashery, S. Conformational Dynamics in Penicillin-Binding Protein 2a of Methicillin-Resistant Staphylococcus aureus, Allosteric Communication Network and Enablement of Catalysis, J. Am. Chem. Soc. 2017, 139, 2102-2110.

348. Light, S. H.; Cahoon, L. A.; Mahasenan, K. V.; Lee, M.; Boggess, B.; Halavaty, A. S.;

Mobashery, S.; Freitag, N. E.; Anderson, W. F. Transferase versus Hydrolase: the Role of Conformational Flexibility in Reaction Specificity, Structure 2017, 25, 295-304.

349. Lee, M.; Hesek, D.; Dik, D. A.; Fishovitz, J.; Lastochkin, E.; Boggess, B.; Fisher, J. F.;

Mobashery, S. From Genome to Proteome to Elucidation of Reactions for All Eleven Known Lytic Transglycosylases from Pseudomonas aeruginosa, Angew. Chem. Int. Ed. 2017, 56, 2735-2739.

350. Acebron, I.; Mahasenan, K.; De Benedetti, S.; Lee, M.; Artola-Recolons, C.; Hesek, D.;

Wang, H.; Hermoso, J.; Mobashery, S. Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa, J. Am. Chem. Soc. 2017, 139, 6795-6798.

351. Mahasenan, K.; Bastian, M.; Gao, M.; Frost, E.; Ding, D.; Zorina-Lichtenwalter, K.; Jacobs,

J.; Suckow, M.; Schroeder, V.; Wolter, W.; Chang, M.; Mobashery, S. Exploitation of Conformational Dynamics in Imparting Selective Inhibition for Related Matrix Metalloproteinases, ACS Med. Chem. Lett. 2017, 8, 654–659.

352. Lee, M.; Hesek, D.; Lastochkin, E.; Dik, D. A.; Boggess, B.; Mobashery, S. Deciphering the

Nature of Enzymatic Modifications of Bacterial Cell Wall, ChemBioChem. 2017, 18, 1696-


32

1702. 353. Dik, D. A.; Marous, D. R.; Fisher, J. F.; Mobashery, S. Lytic Transglycosylases: Concinnity

in Concision of the Bacterial Cell Wall, Crit. Rev. Biochem. Mol. Biol. 2017, 52, 503-542. 354. Meisel, J. E.; Fisher, J. F.; Chang, M.; Mobashery, S. Allosteric Inhibition of Bacterial

Targets: An Opportunity for Discovery of Novel Antibacterial Classes. Top. Med. Chem. 2017 (in press). DOI 10.1007/7355_2017_21.

355. Testero, S.; Granados, C.; Fernández, D.; Gallego, P.; Covaleda, G.; Reverter, D.; Vendrell,

J.; Avilés, F. X. ; Pallarès, I.; Mobashery, S. Discovery of Mechanism-Based Inactivators for Human Pancreatic Carboxypeptidase A from a Focused Synthetic Library, ACS Med. Chem. Lett. 2017 (in press) DOI: 10.1021/acsmedchemlett.7b00346.

356. Horsman, M.; Marous, D.; Li, R.; Oliver, R.; Byun, B.; Emrich, S.; Boggess, B.; Townsend,

C.; Mobashery, S. Whole-Genome Shotgun Sequencing and Comparison of Two β-Proteobacterial Species in Search of the Bulgecin Biosynthetic Cluster, ACS Chem. Biol. 2017 (in press) DOI: 10.1021/acschembio.7b00687

Book: 1. Resolving the Antibiotic Paradox: Progress in Understanding Drug Resistance and

Development of New Antibiotics, Rosen, B.P.; Mobashery, S., Eds.; Plenum Press, NY, 1998.

Patents: 1. Johnston, M. A.; Mobashery, S. Amino Acyl Cephalosporin Derivatives, U. S. Patent

4,783,443 (1988). 2. Mobashery, S. Mechanism-Based Inactivators for Renal Dipeptidase (Dehydropeptidase I)

U. S. Patent 5,112,751 (1992). 3. Mobashery, S. Alkenoic Acid Compounds for Mechanism-Based Inactivation of

Dehydropeptidase Activity U. S. Patent 5,238,930 (1993). 4. Mobashery, S. Alkenoic Acid Compounds for Mechanism-Based Inactivation of

Dehydropeptidase Activity U. S. Patent 5,286,893 (1994). 5. Fridman, R.; Mobashery, S. Inhibitors of Matrix Metalloproteinases, U. S. Patent

6,703,415 (2004). 6. Mobashery, S.; Fridman, F. Inhibitors of Matrix Metalloproteinases, U. S. Patent 7,144,917

(2006). 7. Haddad, J.; Kotra, L.; Mobashery, S. Aminoglycosides as Antibiotics, U. S. Application

7,220,727 B2. US20050171035A1, publication date August4, 2005 8. Mijoon Lee; Masahiro Ikejiri; Mayland Chang; Rafael Fridman; Shahriar Mobashery;

Preparation of thioepoxides as inhibitors ofmatrixmetalloproteinases. U.S. PatentWO2006125208,November23,2006.

9. Mijoon Lee, Masahiro Ikejiri, Mayland Chang, Rafael Fridman, Shahriar Mobashery

Inhibitors of Matrix Metalloproteinases, US Patent 7,928,127; issued April 19, 2011.


33

10. Mayland Chang, Shahriar Mobashery, Mijoon Lee. Gelatinase inhibitors and prodrugs.WO201109767,publicationdate29December2011.

11. Mijoon Lee, Masahiro Ikejiri, Mayland Chang, Rafael Fridman, Shahriar Mobashery.

Inhibitorsofmatrixmetalloproteinases.USPatent8,093,287,issuedJanuary10,2012. 12. Mobashery, S.; Hesek, D.; Chang, M. Phthalanilate Phthalanilate Compounds and Methods

of Use, U. S. Patent 8,859,620., issued October 14, 2014

13. Mobashery, S.; O’Daniel, P.; Chang, M. Antibacterial Compounds and Methods of Using Same, Antibacterial Compounds and Methods of Using Same, US Patent 9,045,442 B2; issued June 2, 2015.

14. Mobashery, S.; O’Daniel, P.I; Chang, M. Antibacterial Compounds and Methods of Using

Same, US Patent 9,045,442; issued June 2, 2015.

1. Shahriar Mobashery, Peter I. O’Daniel, Mayland Chang. Antibacterial compounds and methods of using same. U.S. Patent WO/2009/082398, Publication Date: 02.07.2009 (International Application No. PCT/US2007/088602, International Filing Date: 21.12.2007).

2. Shahriar Mobashery, Peter I. O’Daniel, Mayland Chang. Antibacterial compounds and methods of using same. U.S. Patent WO/2009/041972, Publication Date: 02.04.2009 (International Application No. PCT/US2007/079672, International Filing Date: 27.09.2007).

3. Shahriar Mobashery, Peter I. O’Daniel, Mayland Chang. Antibacterial compounds and methods of using same. U.S. Patent12680541, US2010/0261673A1, filed December 21, 2007, issued June 2, 2015.

15. Chang, M; Mobashery, S.; Lee, M. “Gelatinase Inhibitors and Prodrugs”, US Patent

8,937,151; issued January 20, 2015. 16. Fridman, R.; Mobashery, S. Inhibitors of Matrix Metalloproteinases, European Patent

1,309,579-B1; issued October 12, 2005. 17. Chang, M; Mobashery, S.; Lee, M. “Gelatinase Inhibitors and Prodrugs”, US Patent

9,321,754; issued April 26, 2016. 18. Hesek, D.; Lee, M.; Chang, M.; Mobashery, S. UND-12-005: US Provisional Application

61/522,554 filed 8/11/2011 entitled “Compositions & Diagnostic Methods”. 19. Chang, M.; Suckow, M. A.; Mobashery, S. UND-12-006: US Provisional Application

61/522,544 filed 8/11/2011 entitled “Wound Healing Compositions & Methods”. 20. Chang, M.; Mobashery, S.; Bouley, R. Quinazolinone Antibiotics, International Publication

Number WO 2014/138302 A1. 21. Dantas, G.; Gonzales, P.; Pesesky, M.; Forsberg, K.; Chang, M.; Mobashery, S.,

Compositions and Methods of Use of Antibacterial Drug Combinations, U. S. Patent filed on July 9, 2015

Invited Lectures:


34

1. Purdue University, Department of Chemistry, Identification of Active Site Amino Acid

Residues in Catalytic Subunit of Bovine Cyclic AMP-Dependent Protein Kinase by Peptide-Based Affinity Inactivators, Nov., 1987.

2. Washington University, Department of Chemistry, Identification of Active Site Amino

Acid Residues in Catalytic Subunit of Bovine Cyclic AMP-Dependent Protein Kinase by Peptide-Based Affinity Inactivators, Nov., 1987.

3. Brandeis University, Department of Biochemistry, Identification of Active Site Amino

Acid Residues in Catalytic Subunit of Bovine Cyclic AMP-Dependent Protein Kinase by Peptide-Based Affinity Inactivators, Nov., 1987.

4. Wayne State University, Department of Chemistry, Identification of Active Site Amino

Acid Residues in Catalytic Subunit of Bovine Cyclic AMP-Dependent Protein Kinase by Peptide-Based Affinity Inactivators, Dec., 1987.

5. Salk Institute Biotechnology/Industrial Associates, Active Site Structures of Protein

Kinases, Jan., 1989 6. Wayne State University, Department of Biochemistry, Design of Mechanism-Based

Inactivators for Zinc Proteases, Feb., 1989. 7. Schering-Plough Corporation, New Designs for Aminoglycoside Drugs, July, 1989. 8. Wayne State University, Department of Pharmaceutical Chemistry, Conscripting Active

Site Metals in Metalloproteases in the Chemistry of Mechanism-Based Inactivation., Oct., 1990.

9. Schering-Plough Corporation, Mechanisms of Resistance to β-Lactam and Aminoglycoside

Antibiotics, July, 1991. 10. Department of Medicinal Chemistry, University of Michigan, Mechanisms of Turnover of

Substrates and Irreversible Inactivation by Mechanism-Based Inactivators of Class A β-Lactamases, Ann Arbor, Michigan, October 1991.

11. Department of Biochemistry, Wayne State University, Mechanisms of Turnover of

Substrates and Irreversible Inactivation by Mechanism-Based Inactivators of Class A β-Lactamases, Detroit, Michigan, January 1992.

12. Regeneron Pharmaceuticals, Inc., Mechanistic Processes of Class A β-Lactamases,

Tarrytown, New York, March 1992. 13. The Fifth β-Lactamase Workshop, A Structure-Based Insight into the Inactivation

Chemistry of Class A β-Lactamases by Clavulanate, Holy Island, England, April 1992. 14. Department of Chemistry, University of Cincinnati, Biochemical Basis for Bacterial

Resistance to β-lactam Antibiotics, November 1992. 15. Department of Nutrition and Food Sciences, Wayne State University, A Structure-Based

Analysis of the Processes of the Class A β-Lactamases, November 1992. 16. Department of Chemistry, Wayne State University, A Structure-Based Analysis of the

Processes of the Class A β-Lactamases, November 1992.


35

17. The Upjohn Co., A Structure-Based Analysis of the Processes of the Class A β-

Lactamases, February 1993. 18. Ajinomoto Co., β-Lacam Drug Resistance in Bacteria: Mechanistic Insight into the

Processes of Class A β-Lactamases, Kawasaki, Japan, June 1993. 19. Ono Pharmaceutical Co., Conscripting the Catalytic Machinery of Enzymes in

Development of Pharmaceuticals: Rational Design of the First Generation of Mechanism-Based Inactivators for Zinc Proteases, Osaka, Japan, June 1993.

20. Protein Engineering Research Institute, β-Lactam Drug Resistance in Bacteria: Mechanistic

Insight into the Processes of Class A β-Lactamases, Osaka, Japan, June 1993. 21. Suntory Biomedical Institute, A Structure-Based Analysis of the Processes of the Class A

β-Lactamases, Osaka, Japan, June 1993. 22. Second International Symposium on Bioorganic Chemistry, Mechanistic Insight from

Modeling on the Inactivation Chemistry of β-Lactamases by Clavulanate, Fukuoka, Japan, June 1993.

23. Department of Chemistry, Scripps Institute, Overcoming Resistance to β-Lactam Drugs, La

Jolla, California, November 1993. 24. University of Detroit, Department of Chemistry, A Structure-Based Analysis of the

Processes of the Class A β-Lactamases, January 1994. 25. Wayne State University, Department of Pharmacology, A Structure-Based Analysis of the

Processes of the Class A β-Lactamases, January 1994. 26. Schering-Plough Corporation, Mechanisms of Resistance to β-Lactam and Aminoglycoside

Antibiotics, January 1994. 27. Department of Biological Chemistry, University of Michigan, A Structure-Based Analysis

of the Processes of the Class A β-Lactamases, The Enzyme Discussion Group, February 1994.

28. University of California at Santa Cruz, A Structure-Based Analysis of the Processes of the

Class A β-Lactamases, Department of Chemistry, February 1994. 29. Department of Chemistry, University of Minnesota, A Structure-Based Analysis of the

Processes of the Class A β-Lactamases, March 1994. 30. The joint 26th Central Regional/27th Great Lakes Regional ACS meeting, Mechanism-

Based Inactivation of Zinc Proteases, Ann Arbor, Michigan, June 1994. 31. Gordon Conference on Enzymes, Cofactors, and Metabolic Pathways, Overcoming

Resistance to β-Lactam Drugs: Novel Strategies for Inhibition of β-Lactamases, New Hampshire, July 1994.

32. Department of Chemistry, State University of New York at Buffalo, A Structure-Based

Analysis of the Processes of the Class A β-Lactamases, September 1994.


36

33. Department of Chemistry, Michigan Technological University, A Structure-Based Analysis of the Processes of the Class A β-Lactamases, September 1994.

34. American Society for Microbiology National Meeting, Prospect for the Use of β-

Lactamase Inhibitors in Clinic for the Next 15 Years; Orlando, Florida, October 1994. 35. Department of Chemistry, Indiana University (Bloomington), A Structure-Based Analysis

of the Processes of the Class A β-Lactamases, November 1994. 36. SmithKline-Beecham Pharmaceutical Co., A Structure-Based Analysis of the Processes of

the Class A β-Lactamases, Brockham Park, UK, November 1994. 37. Department of Chemistry, University of Exeter, A Structure-Based Analysis of the

Processes of the Class A β-Lactamases, Exeter, UK, November 1994. 38. Department of Biochemistry, University of Liège, Mecanismes de Resistance des β-Lactam

Antibiotiques Causés par le TEM β-Lactamase, Liège, Belgium, November 1994. 39. Department of Chemistry, Ecole Supérieure de Chimie Industrielle de Lyon, Mecanismes

de Resistance des β-Lactam Antibiotiques Causés par le TEM β-Lactamase, Lyon, France, November 1994.

40. Laboraroire de Pharmacologie et de Toxicologie Fondamentales, Centre National de la

Recherche Scientifique, S., Mecanismes de Resistance des β-Lactam Antibiotiques Causés par le TEM β Lactamase, Toulouse, France, November 1994.

41. Cornell University School of Medicine, Molecular Basis for Bacterial Resistance to β-

Lactam Antibiotics, New York, December 1994. 42. Department of Chemistry, Oakland University, Resistance to β-Lactam Antibiotics,

January 1994. 43. The First International Workshop on Enzyme Inhibitor Design, Design of Mechanism-

Based Enzyme Inactivators as Potential Pharmaceuticals, Pohang, Korea, February 1995. 44. Dong-A Pharmaceutical Co., Design of Mechanism-Based Enzyme Inactivators as

Potential Pharmaceuticals, Seoul, Korea, February 1995. 45. The Sixth β-Lactamase Workshop, Holy Island, Novel Mechanism-Based Inhibitors for β-

Lactamases, UK, April 1995. 46. Plenary Lecture, 13th Summer Symposium on Organic Synthesis, Mobashery, S., Design

and Synthesis of Biologically Active Compounds, Fukuoka city, Japan, July 1995. 47. Kyoto Pharmaceutical University, Department of Medicinal Chemistry, Overcoming

Resistance to Antibiotic, Kyoto, Japan, August 1995. 48. Osaka University, Faculty of Pharmaceutical Sciences, Overcoming Resistance to

Antibiotic, Osaka, Japan, August 1995. 49. Suntory Institute for Bioorganic Research, Overcoming Resistance to Antibiotic, Osaka,

Japan, August 1995.


37

50. Affymax Corp., Overcoming Resistance to Antibiotic, Santa Clara, California, September 1995.

51. 35th Interscience Conference on Antimicrobial Agents and Chemotherapy, Turnover of the

Fourth-Generation Cephalosporin Cefepime by the TEM-1 β-Lactamase: Evidence for Conformational Flexibility of Enzyme, San Francisco, September 1995.

52. Department of Chemistry, Case Western Reserve University, Cleveland, Chemical

Strategies for Overcoming Resistance to Antibiotics, Ohio, September 1995. 53. Pharmacia-Upjohn Co., Overcoming Resistance to Antibiotic, Kalamazoo, MI, November

1995. 54. International Chemical Congress of Pacific Basin Societies, Overcoming Resistance to

Antibiotic, Honolulu, December 1995. 55. Wyeth-Ayerst Research/Lederle laboratories, Mechanisms of β-Lactamases and the

Challenge of Inhibition, Pearl River, New York, March 1996. 56. School of Pharmaceutical Sciences, Beijing Medical University, The People's Republic of

China, Mechanisms of β-Lactamases and the Challenge of Inhibition, May 1996. 57. National Laboratory of Natural and Biomimetic Drugs, Beijing Medical University, The

People's Republic of China, Beta-lactamases: Evolution of a Versatile Bacterial Catalyst, May 1996.

58. Interscience Conference on Antimicrobial Agents and Chemotherapy, Mechanism of

Deacylation for Class A β-Lactamases, New Orleans, Louisiana, September 1996. 59. Schering-Plough Corp., Overcoming Resistance to Antibiotic, Kenilworth, NJ, October

1996. 60. Sixteenth Midwest Enzyme Chemistry Conference, Chicago, Illinois, Evolution of the

Versatile β-lactam Hydrolase Activity: From Biosynthetic enzymes to Drug Resistance Factors, October 1996.

61. Case Western Reserve University, Department of Pharmacology, Evolution of the Versatile

β-lactam Hydrolase Activity: From Biosynthetic enzymes to Drug Resistance Factors, October 1996.

62. Stanford University, Department of Chemistry, Evolution of the Versatile β-lactam

Hydrolase Activity: From Biosynthetic enzymes to Drug Resistance Factors, November 1996.

63. University of Michigan at Dearborn, Overcoming Resistance to Antibiotic, November

1996. 64. Wayne State University, Department of Chemistry, Frontiers of Science Lecture Series,

Evolution of the Versatile β-lactam Hydrolase Activity: From Biosynthetic Enzymes to Drug Resistance Factors, December 1996.

65. Affymax Corp., Santa Clara, California, Evolution of the Versatile β-lactam Hydrolase

Activity: From Biosynthetic Enzymes to Drug Resistance Factors, December 1996.


38

66. McMaster University, Department of Biochemistry, Hamilton, Ontario, Canada, Evolution of the Versatile β-lactam Hydrolase Activity: From Biosynthetic Enzymes to Drug Resistance Factors, December 1996.

67. University of Waterloo, Department of Chemistry, Waterloo, Ontario, Canada, Evolution

of the Versatile β-lactam Hydrolase Activity: From Biosynthetic Enzymes to Drug Resistance Factors, December 1996.

68. Schering-Plough Corp., Kenilworth, New Jersey, Cephalosporin-Aminoglycoside Conjoint

Antibacterials, December 1996. 69. Southern Methodist University, Department of Chemistry, Dallas, Texas, Evolution of the

Versatile β-lactam Hydrolase Activity: From Biosynthetic Enzymes to Drug Resistance Factors, January 1997.

70. University of Texas, Department of Chemistry, Arlington, Texas, Evolution of the


71. Duke University, Department of Chemistry, Durham, North Carolina, Evolution of the


72. Bristol-Myers Squibb, Wallingford, Connecticut, Bacterial β-lactamases: Nuances of

Mechanisms and Challenge of Inhibition, March 1997. 73. Universität des Saarlandes, Department of Pharmaceutical Chemistry, Overcoming

Resistance to Antibiotic, Saarbrücken, Germany, March 1997. 74. University of Bern, Department of Chemistry, Evolution of Versatile Bacterial Catalysts:

From Biosynthetic enzymes to Drug Resistance Factors, Bern, Switzerland, April 1997. 75. Hoffmann-La Roche Pharmaceutical Co., Evolution of Versatile Bacterial Catalysts: From

Biosynthetic enzymes to Drug Resistance Factors, Basel, Switzerland, April 1997. 76. Centre National de la Recherche Scientifique, Toulouse, France, Evolution of the Versatile

β-lactam Hydrolase Activity: From Biosynthetic Enzymes to Drug Resistance Factors, April 1997.

77. University of Toledo, Department of Medicinal Chemistry, Bacterial β-lactamases:

Nuances of Mechanisms and Challenge of Inhibition, April 1997. 78. Symposium on Antibacterial Drug Resistance and New Developments in Antibiotics,

Wayne State University, "Enzymes of Drug Resistance", May 1997. 79. Gordon Conference on Bioorganic Chemistry, "Evolution of the Versatile β-lactam

Hydrolase Activity: from Biosynthetic enzymes to Drug Resistance Factors ", Andover, New Hampshire, June 1997.

80. Abbott Pharmaceutical Co., "Bacterial β-lactamases: Nuances of Mechanisms and

Challenge of Inhibition, July 1997.


39

81. Procter & Gamble Pharmaceuticals, "Evolution of the Versatile β-lactam Hydrolase Activity: from Biosynthetic enzymes to Drug Resistance Factors ", Cincinnati, Ohio, August 1997.

82. Notre Dame University, "Evolution of the Versatile β-lactam Hydrolase Activity: From

Biosynthetic enzymes to Drug Resistance Factors", Notre Dame, Indiana, September, 1997.

83. Department of Biochemistry, WSU, "Evolution of the Versatile β-lactam Hydrolase

Activity: from Biosynthetic enzymes to Drug Resistance Factors", Detroit, MI, October 1997.

84. The Fifth International Symposium on Protease Inhibitors and Biological Control,

"Computational Insight into Structures, Substrate Preference and Inhibition by Protein Inhibitors of Human Gelatinases", Brdo, Slovenija, October, 1997.

85. Department of Biochemistry, Albert Einstein College of Medicine, "Evolution of the

Versatile β-lactam Hydrolase Activity: from Biosynthetic enzymes to Drug Resistance Factors", October 1997.

86. Consiglio Nazionale delle Ricerche, "Evolution of the Versatile β-lactam Hydrolase

Activity: from Biosynthetic enzymes to Drug Resistance Factors", Bologna, Italy, October 1997

87. Kresge Eye Institute, "Evolution of the Versatile β-lactam Hydrolase Activity: from

Biosynthetic enzymes to Drug Resistance Factors", Detroit, MI, November 1997. 88. Wyeth-Ayerst Research/Lederle laboratories"Evolution of the Versatile β-lactam

Hydrolase Activity: from Biosynthetic enzymes to Drug Resistance Factors", Pearl River, New York, January 1998.

89. Aurora Biosciences Corporation, "Evolution of the Versatile β-lactam Hydrolase Activity:

from Biosynthetic enzymes to Drug Resistance Factors", San Diego, CA, March 1998. 90. Hoechst-Marion-Roussel Pharmaceutical Co, "Evolution of the Versatile β-lactam

Hydrolase Activity: from Biosynthetic enzymes to Drug Resistance Factors", Paris, France, March 1998.

91. Institut de Pharmacologie et de Biologie Structurale, "Evolution of the Versatile β-lactam

Hydrolase Activity: from Biosynthetic enzymes to Drug Resistance Factors", Toulouse, France, March 1998.

92. Oxford University, The Centre for Molecular Sciences, "Bacterial β-lactamases: Nuances

of Mechanisms and Challenge of Inhibition", Oxford, U.K., April 1998. 93. The Seventh β-Lactamase Workshop, "Structural and Mechanistic Implications for

Evolution of β-Lactamases from Penicillin-Binding Proteins", Holy Island, UK, April 1998.

94. Department of Pharmacology, Wayne State University, "Structural and Mechanistic

Implications for Evolution of β-Lactamases from Penicillin-Binding Proteins", April 1998. 95. Bristol-Myers Squibb, Wallingford, Connecticut, "Selection of Novel Resistance to

Expanded-Spectrum β-Lactam Antibiotics", August 1998.


40

96. Symposium on Unravelling the Biological and Pathological Functions of Proteolytic

Enzymes, Wayne State University School of Medicine, “Strategies for Inhibition of Proteases”, October, 1998.

97. Schering Plough Corp., “Antibiotics: The Twentieth-Century "Silver Bullets" and How

They Are Being Tarnished", November 1998. 98. Southern Illinois University, Department of Chemistry, "Evolution of the Versatile β-

lactam Hydrolase Activity: from Biosynthetic enzymes to Drug Resistance Factors", January 1999.

99. Washington University, Department of Chemistry, “Antibiotics: The Twentieth-Century

Miracle Drugs and How They Are Being Tarnished", January 1999. 100. Ohio State University of "Structural and Mechanistic Implications for Evolution of β-

Lactamases from Penicillin-Binding Proteins", April, 1999. 101. Georgia Institute of Technology, “Antibiotics: The Twentieth-Century "Silver Bullets" and

How They Are Being Tarnished", April, 1999. 102. International Meeting on β-Lactamase-Mediated Resistance: Molecular Aspects and

Clinical Implications, L'Aquila, "Structural and Mechanistic Bases for Evolution of β-Lactamases", Italy, June 1999.

103. Department of Chemistry, Universitad Islas Baleares, "Modelización de Interacciones

Enzima-Sustrato", Palma Mallorca, Spain, June 1999. 104. University of Grenole, Grenoble, France, “Antibiotics: The Twentieth-Century "Silver

Bullets" and How They Are Being Tarnished", June 1999. 105. Consiglio Nazionale delle Ricerche, "Chemical Strategies is Design of Inhibitors for

Proteases", Bologna, Italy, June 1999. 106. Interscience Conference on Antimicrobial Agents and Chemotherapy, “High-Resolution

Imaging of the Assembly of the Bacterial Outer-membrane”, San Francisco, California, September 1999.

107. University of Iowa, “Antibiotics: The Twentieth-Century "Silver Bullets" and How They

Are Being Tarnished", September, 1998. 108. International Proteolysis Society: Proetase Consortium, Mackinac, Michigan, “Strategies

for Protease Inhibition”, October 1999. 109. Loyola University of Chicago, "Antibiotics: Twentieth Century "Magic Bullets" and How

They are being tarnished", Chicago, November 1999. 110. The Second International Conference on Protease Inhibitors, Gainsville, “New

Methodology for Inhibition of Proteases”, December 1999. 111. University of Alberta, "Structural and Mechanistic Implications for Evolution of β-

Lactamases from Penicillin-Binding Proteins", Edmonton, Canada, December 1999.


41

112. Michigan State University, Department of Biochemistry, "Structural and Mechanistic Implications for Evolution of β-Lactamases from Penicillin-Binding Proteins", February 2000.

113. Purdue University, Department of Medicinal Chemistry, "Structural and Mechanistic

Implications for Evolution of β-Lactamases from Penicillin-Binding Proteins", March 2000.

114. Launching Ceremony for the Institute for Scientific Computing, Wayne State University,

“Drug Discovery and Computational Chemistry”, April 2000. 115. Cerus Science Retreat: New Opportunities & Competing Technologies, "Overcoming

Resistance to Antibiotics", Santa Cruz, California, May 2000. 116. Guilford Pharmaceutical Company, “Methodology for Mechanism-based Inhibition of Zinc-

Dependent Proteases”, Baltimore, June 2000. 117. Gordon Research Conference on Enzymes, Coenzyme, and Metabolic Pathways, "Cross

linking of the bacterial cell wall by penicillin-binding proteins, and how this activity has given rise to antibiotic resistant determinants", July 2000.

118. University of Michigan, "Cross linking of the bacterial cell wall by penicillin-binding

proteins, and how this activity has given rise to antibiotic resistant determinants", September 2000.

119. Wayne State University, Department of Pharmacology, "Cross linking of the bacterial cell

wall by penicillin-binding proteins, and how this activity has given rise to antibiotic resistant determinants", October 2000.

120. Vanderbilt University, “β-Lactam Antibiotics: The Twentieth-Century "Silver Bullets" and

How They Are Being Tarnished", October 2000. 121. The Developmental Therapeutics Program, WSU, “β-Lactam Antibiotics: The Twentieth-

Century "Silver Bullets" and How They Are Being Tarnished", November 2000. 122. Michigan State University, "Cross linking of the bacterial cell wall by penicillin-binding

proteins, and how this activity has given rise to antibiotic resistant determinants", December 2000.

123. International Chemical Congress of Pacific Basin Societies (“Pacifichem 2000”),

"Antibiotics: Twentieth Century "How Bacteria Cross-Link Their Cell Walls: Target for Antibiotics", Honolulu, December 2000.

124. DARPA, “Bacterial Envelope”, San Francisco, January 2001. 125. Karmanos Cancer Institute, “Gelatinases and Cancer Metastasis: Insights into the Complex

Processes of Enzyme Inhibition and Zymogen Activation”, February 2001.


42

126. University of Western Ontario, “β-Lactam Antibiotics: The Twentieth-Century "Silver Bullets" and How They Are Being Tarnished", February 2001.

127. Florida State Universitry, “Gelatinases and Cancer Metastasis: Insights into the Complex

Processes of Enzyme Inhibition and Zymogen Activation”, March 2001 128. Keynote Lecture, Bioferma Chair Lectureship, University of Murcia, Spain, Antibioticos:

El Milagro Medico del Siglo Veinte y Como Estan Perdiendo Efectividad Terapeutica", March 2001.

129. University of Murcia, Spain, "Cross linking of the bacterial cell wall by penicillin-binding

proteins, and how this activity has given rise to antibiotic resistant determinants", March 2001.

130. University of the Baleares Islands, Spain, "Cross linking of the bacterial cell wall by

penicillin-binding proteins, and how this activity has given rise to antibiotic resistant determinants", March 2001.

131. Indiana University, "Cross linking of the bacterial cell wall by penicillin-binding proteins,

and how this activity has given rise to antibiotic resistant determinants", March 2001. 132. Plenary Lecture, National Meeting of the Korea Chemical Society, Seoul, Korea, “Matrix

Metalloproteinases: Sturctures, Function, and Inhibition”, April 2001. 133. Symposium on Chemical Genomics, Pohang University of Science and Technology,

Pohang, Korea, “Cross linking of the bacterial cell wall by penicillin-binding proteins, and how this activity has given rise to antibiotic resistant determinants”, April 2001.

134. DuPont Pharmaceuticals Co., "Cross linking of the bacterial cell wall by penicillin-binding

proteins, and how this activity has given rise to antibiotic resistant determinants", Wilmington, April 2001.

135. NewBiotics Pharmaceuticals Co., "Cross linking of the bacterial cell wall by penicillin-

binding proteins, and how this activity has given rise to antibiotic resistant determinants", San Diego, April 2001.

136. Trends in Drug Research, 13th Noordwijkerhout-Camerino Symposium, “Antibiotic Design

for Validated Targets”, Noordwijkerhout, Netherlands, May 2001. 137. The 101th General Meeting of the American Society for Microbiology, “Bichemical and

Structural Insights into Class D β-lactamases”, Orlando, May 2001. 138. Plenary Lecture, in Trends in Organic Chemistry of the Swedish Royal Academy of

Sciences, “Antibacterials as Wonder Drugs and How Their Effectiveness Is Being Compromised”, Stockholm, Sweden, May 2001.

139. American Chemical Society, Great Lakes Regional Meeting, “Novel Aminoglycosides by

Design”, Grand Rapids, June 2001. 140. The 222nd National Meeting of the American Chemical Society, Symposium on

"Inhibition of Enzymes Important in Medicine", “Matrix metalloproteinases: structures, function, and inhibition", Chicago, Illinois, August 2001.


43

141. Bioinformatics and Structural Modeling Workshop, Istanbul, Turkey, "Applications of Molecular Modeling to Systems of Importance to Biological Sciences", September 2001.

142. Institute of Molecular Chemistry, University of Amsterdam, The Netherlands “Cancer

Metastasis and Matrix metalloproteinases: structures, function, and inhibition", September 2001.

143. Department of Chemistry, University of Montreal, “Antibacterials as Wonder Drugs and

How Their Effectiveness Is Being Compromised”, Montreal, Canada, December 2001. 144. Frontiers of Science Lecture, Department of Chemistry, Wayne State University, “Matrix

metalloproteinases: structures, function, and inhibition”, January 2002. 145. National Institute of Child Health, Perinatology Research Branch, “Matrix

metalloproteinases: structures, function, and inhibition”, January 2002. 146. National Academy of Sciences, Institute of Medicine, Forum on Emerging Infections,

Washington, D.C., Emergence of Multiple Mechanisms of Resistance to Antibacterials, February 2002.

147. Ohio Sate University, Department of Biochemistry, “Antibacterials as Wonder Drugs and

How Their Effectiveness Is Being Compromised”, March 2002. 148. The Eight β-Lactamase Workshop, "Inhibitor-Resistant β-Lactamases", Holy Island, UK,

March, 2002. 149. Case-Western Reserve University, Department of Pharmacology, “Antibacterials as

Wonder Drugs and How Their Effectiveness Is Being Compromised”, April 2002. 150. Frontiers in Medicinal Chemistry Lecture, University of Utah, “Antibacterials as Wonder

Drugs and How Their Effectiveness Is Being Compromised”, April 2002. 151. The 223rd National Meeting of the American Chemical Society, Symposium on

"Carbohydrate Chemistry", “Retailoring Aminoglycoside Antibiotics Based on Ribosomal Target Structure and Mechanistic Considerations", Orlando, April 2002.

152. Antimicrobial Research Centre, McMaster University, Canada, “Antibacterials as Wonder

Drugs and How Their Effectiveness Is Being Compromised”, May 2002. 153. University of Toronto, Canada, “Antibacterials as Wonder Drugs and How Their

Effectiveness Is Being Compromised”, May 2002. 154. International Conferewnce on Genomics, Proteomics and Bioinformatics, “Design of Novel

Antibiotics that Bind to the Bacterial Ribosomal Acyltransfer Site”, St Petersburg, Russia, June 2002.

155. ImClone Corp., “Matrix Metalloproteinases and Their Involvement in Cancer Metastasis",

New York, August 2002. 156. The 224rd National Meeting of the American Chemical Society, Symposium on

"metalloproteases", “Matrix Metalloproteinases and Their Involvement in Cancer Metastasis", Boston, August 2002.


44

157. Washington State University, Department of Chemistry, “Antibacterials as Wonder Drugs and How Their Effectiveness Is Being Compromised”, September 2002.

158. University of Connecticut, “Protein and Polymer Science in the 21st Century” Symposium

in the Honor of Professor James Knox, “Antibacterials as Wonder Drugs and How Their Effectiveness Is Being Compromised”, September 2002.

159. University of Washington, Department of Chemistry, “Antibacterials as Wonder Drugs and

How Their Effectiveness Is Being Compromised”, October 2002. 160. University of Notre Dame, Department of Chemistry and biochemistry, “Antibacterials as

Wonder Drugs and How Their Effectiveness Is Being Compromised”, October 2002. 161. Pharmacia Symposium on Molecular Target-Based Cellular and Animal Models,

“Antibacterials as Wonder Drugs and How Their Effectiveness Is Being Compromised”, October 2002.

162. Tufts University, Department of Chemistry, “Antibacterials as Wonder Drugs and How

Their Effectiveness Is Being Compromised”, October 2002. 163. Ohio Wesleyan University, Department of Chemistry, “Antibacterials as Wonder Drugs

and How Their Effectiveness Is Being Compromised”, November 2002. 164. Purdue University, Department of Chemistry, “Antibacterials as Wonder Drugs and How

Their Effectiveness Is Being Compromised”, November 2002. 165. Baylor College of Medicine, “Antibacterials as Wonder Drugs and How Their

Effectiveness Is Being Compromised”, January 2003. 166. Center for Biological Modeling, Michigan State University, “Antibacterials as Wonder

Drugs and How Their Effectiveness Is Being Compromised”, January 2003. 167. University of Washington, “Antibacterials as Wonder Drugs and How Their Effectiveness

Is Being Compromised”, February 2003. 168. Chemistry Colloquia, University of Nebraska, “Antibacterials as Wonder Drugs and How

Their Effectiveness Is Being Compromised”, April 2003. 169. Fargo Conference on Metalloproteinases, “Inhibition and Activation of Gelatinases”,

Fargo, North Dakota, May 2003. 170. IUPAC Symposium on New Targets for Antibacterials, “New Designer Antibiotics; Old

and New Targets”, Amsterdam, Netherlands, June 2003. 171. Rigel Inc., “Antibacterials as Wonder Drugs and How Their Effectiveness Is Being

Compromised”, South San Francisco, July 2003. 172. Symposium on “Biomolecular Structure, Cellular Structure and Drug Discovery”,

International Union of Biochemistry and Molecular Biology Congress, Toronto, Canada, “Antibacterials as Wonder Drugs and How Their Effectiveness Is Being Compromised”, July 2003.

173. Gordon Research Conference on Matrix Metalloproteinases, "Contributions of Molecular

Dynamics to Biochemistry of MMPs", Big Sky, Montana, August 2003.


45

174. Science Advisory Council, University of Notre Dame, “Science at the Interface of

Chemistry and Biology”, September 2003. 175. Plenary Lecture, The XIV National Symposium in Organic Chemistry of the Argentinian

Society of Organic Chemistry, “Antibioticos: El Milagro Medico del Siglo Veinte y Como Estan Perdiendo Efectividad Terapeutica”, Rosario, Argentina, November 2003.

176. Instituto de Biologia de Rosario, “Antibacterials as Wonder Drugs and How Their

Effectiveness Is Being Compromised”, Rosario, Argentina, November 2003. 177. Chemistry Colloquium Speaker, Wichita State University, “Antibacterials as Wonder

Drugs and How Their Effectiveness Is Being Compromised”, December 2003. 178. Andrews University, "Bacterial Cell Wall, the Ribosome, and Antibiotics", March 2004. 179. Chemical Biology Lecture Series, University of Illinois at Urbana-Champaign,

“Antibacterials as Wonder Drugs and How Their Effectiveness Is Being Compromised”, April 2004.

180. The 14th European Congress of Clinical Microbiology and Infectious Diseases (ECCMID),

“Resistance to β-Lactam Antibiotics in Staphylococcus aureus”, Prague, Czech Republic, May 2004.

181. University of Parma, "Bacterial Cell Wall, the Ribosome, and Antibiotics", May 2004. 182. National Meeting of the American Society for Microbiology, “BlaR of Staphylococcus

aureus and Its Involvement in Signal Transduction of Antibiotic Resistance”, New Orleans, May 2004.

183. Second Chianti Meeting on Proteases, “Design and Synthesis of a Selective Mechanism-

Based Inhibitor for Gelatinases, Which Inhibit Metastasis in a Mouse Model of T-Cell Lymphoma”, Siena, May 2004.

184. Symposium on “Biomolecular Structure, Cellular Structure and Drug Discovery”,

International Union of Biochemistry and Molecular Biology Congress, Toronto, Canada, “Drug Design at the Interface of Chemistry and Biology”, July 2004.

185. Plenary Lecture, International Symposium on the Frontiers of Chemistry in Honor of

Professor Dong Kim, Pohang University of Science and Technology, "Bacterial Cell Wall, the Ribosome, and Antibiotics", Pohang, Republic of Korea, August 2004.

186. Walther Cancer Institute Retreat, “Design and Synthesis of a Selective Mechanism-Based

Inhibitor for Gelatinases, Which Inhibit Metastasis and Proliferation in Animal Models for Lymphoma and Prostate Cancer”, Notre Dame, August 2004.

187. International Meeting on Inhibition of Matrix Metalloproteinases: Expanding the Horizons,

“Design and Synthesis of a Selective Mechanism-Based Inhibitor for Gelatinases”, New York City, October 2004.

188. Northwestern University, "Bacterial Cell Wall, the Ribosome, and Antibiotics", November

2004.


46

189. University of Kentucky, "Bacterial Cell Wall, the Ribosome, and Antibiotics", March 2005.

190. The 9th β-Lactamase Meeting, “Bacterial Cell Wall”, Leonessa, Italy, June 2005. 191. The 9th β-Lactamase Meeting, “Crystal Structure of the Acylated β-Lactam Sensor Domain

of BlaR1 from Staphylococcus aureu”, Leonessa, Italy, June 2005. 192. The Burnham Institute, "Mechanism-Based Approaches for Biological Intervention of

Disease", San Diego, July 2005. 193. Schering-Plough Corp, “Design, Synthesis and Evaluation of a Selective Mechanism-Based

Inhibitor for Gelatinases as a Strategy in Intervention of Cancer Metastasis", Cambridge, MA, August 2005.

194. National Meeting of the American Chemical Society, “Circumventing Antibiotic

Resistance”, Washington DC, September 2005. 195. New Developments in Synthetic Organic Chemistry of Natural Product and Medicine,

"Bacterial Cell Wall, the Ribosome, and Antibiotics", Kyoto, Japan, September 2005. 196. University of Osaka, School of Pharmacy, "Bacterial Cell Wall, the Ribosome, and

Antibiotics", Osaka, Japan, September 2005. 197. University of Osaka, Graduate School of Medicine, “Evaluation of a de Novo Designed

Selective Mechanism-Based Inhibitor for Gelatinases as a Strategy in Intervention of Cancer Metastasis and Alleviation of the Consequences of Stroke”, Osaka, Japan, September 2005.

198. Osaka Prefecture University, "Bacterial Cell Wall, the Ribosome, and Antibiotics", Osaka,

Japan, September 2005. 199. World High Technology Society 3rd Annual Congress, Shanghai, China, October, 2005 200. University of California at San Diego, "Bacterial Cell Wall, the Ribosome, and

Antibiotics", January 2006. 201. Frontier of Science Lecture, Case-Western University, "Bacterial Cell Wall, the Ribosome,

and Antibiotics", January 2006. 202. University of Minnesota, Department of Medicinal Chemistry, "Bacterial Cell Wall, the

Ribosome, and Antibiotics", February 2006. 203. University of Hong Kong, Department of Chemistry, "Bacterial Cell Wall, the Ribosome,

and Antibiotics", April 2006. 204. Hong Kong University of Science and Technology, "Bacterial Cell Wall, the Ribosome,

and Antibiotics", May 2006. 205. University of Hong Kong, Department of Microbiology, "Emergence of Staphylococcus

aureus as a Clinical Scourge", May 2006. 206. University of Minnesota, Center for Drug Design, "Emergence of Staphylococcus aureus

as a Clinical Scourge", June 2006.


47

207. Merck & Co., "Emergence of Staphylococcus aureus as a Clinical Scourge", Rahway, NJ,

August 2006. 208. American Chemical Society National Meeting, “Synthesis and Three-Dimensional

Structure of a Fragment of the Bacterial Cell Wall Peptidoglycan”, San Francisco, September 2006.

209. North Eastern Structure Symposium: Structural Insights into Macromolecular Assemblies,

“Three-Dimensional Structure of the Bacterial Cell Wall Peptidoglycan”, University of Connecticut, September 2006.

210. Northern Illinois University, “Resistance to β-Lactam Antibiotics in Methicillin-Resistant

Staphylococcus aureus (MRSA)", January 2007. 211. Delhi University, Department of Chemistry, "Chemistry of Resistance to β-Lactam

Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)", New Delhi, India, March 2007.

212. Third International Symposium on Current Trends in Drug Discovery Research, “Control

of Extra-cellular Matrix Degradation by Small Molecules in Prevention of Disease”, Lucknow, India, February 2007.

213. Second International Conference on Pharmaceutical Sciences & Practice, “Control of

Extra-cellular Matrix Degradation by Small Molecules in Prevention of Disease”, Ooty, India, February 2007.

214. University of Montreal, Department of Chemistry, "Chemistry of Resistance to β-Lactam

Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)", Montreal, Canada, March 2007.

215. The Merck Frosst Lecture, Simon Fraser University, "Bacterial Cell Wall, the Ribosome,

and Antibiotics", Vancouver, Canada, March 2007. 216. The Rising Lecture, Oregon State University, “Chemistry of Resistance to β-Lactam

Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, April 2007. 217. IUPAC Symposium on New Targets for Antibacterials, “The Mec and Bla Operons and

Resistance to Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)", April 2007.

218. The Ohio State University, Department of Chemistry Colloquium, "Chemistry of

Resistance to β-Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)", April 2007.

219. The 107th General Meeting of the American Society for Microbiology, “Regulation of β-

Lactam Antibiotic Resistance in Methicillin-Resistant Staphylococcus aureus and Its Origins", Toronto, Cananda, May 2007.

220. International Conference on the Chemistry of Antibiotics and other Bioactive Compounds

(ICCA-10), "Bacterial Cell Wall", Vanderbilt University, August 2007. 221. Albany Molecular, “Bacterial Cell Wall and Antibiotics”, September 2007.


48

222. University of Pennsylvania, “Bacterial Cell Wall”, October 2007. 223. Pasteur Institute, French Society of Microbiology, “Antibiotic Resistance Mechanisms in

Methicillin-Resistant Staphylococcus Aureus”, Paris, France, December 2007. 224. The Peptidoglycan Symposium at the University of Wisconsin, “Structure of the Bacterial

Peptidoglycan”, December 2007. 225. University of California, Davis, “Bacterial Cell Wall and Antibiotics”, Jan 2008. 226. University of New Orleans, “Bacterial Cell Wall and Antibiotics”, Jan 2008. 227. Grand Valley State University, “Bacterial Cell Wall”, Feb. 2008. 228. Vanderbilt University Institute for Chemical Biology, “Chemistry of Resistance to β-

Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, Jan 2008. 229. Keynote Speaker, The 28th Annual Symposium in the Pharmacological Sciences and

Biorelated Chemistry, University of Michigan, “Chemistry of Resistance to β-Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, March 2008.

230. American Chemical Society National Meeting, “Role of the Active Site Zinc Ion of Matrix

Metalloproteinases in Enzyme Activation and Its Subversion in the Process of Selective Inhibition”, New Orleans, April 2008.

231. Merck & Co., "Bacterial Cell Wall", Rhaway, NJ, April 2008. 232. University of New Orleans, "Bacterial Cell Wall", New Orleans, April 2008. 233. The 10th β-Lactamase Meeting, “Penicillin-Binding Protein 5 of Escherichia coli and Its

Implications for β-Lactamases, Eretria, Greece, June 2008. 234. Universitat Autonoma de Barcelona, “Mechanism of Matrix Metalloproteinase Activation

and the Process of Selective Inhibition”, Barcelona, Spain, June 2008. 235. Molecular Biology Institute of Barcelona (CSIC), “Resistance to β-Lactam Antibiotics in

Methicillin-Resistant Staphylococcus aureus (MRSA)”, Barcelona, Spain, June 2008. 236. Instituto de Quimica-Fisica Rocasolano, Spanish National Research Council, "Bacterial

Cell Wall", Madrid, Spain, June 2008. 237. NovaBay Pharmaceuticals, Inc., “Resistance to β-Lactam Antibiotics in Methicillin-

Resistant Staphylococcus aureus (MRSA)”, Emeryville, CA, July 2008. 238. Theravance Pharmaceutical Co., "Bacterial Cell Wall", San Francisco, CA, Aug. 2008. 239. The Astellas Award Lecture, American Chemical Society National Meeting, "Bacterial

Cell Wall", Philadelphia, August 2008. 240. Plenary Lecture, The XII International Congress of Bacteriology and Applied

Microbiology of the International Union of Microbiology Societies (IUMS), “Bacterial Cell Wall, Its Regulation and Involvement in Antibiotic Resistance”, Istanbul, Turkey, August, 2008.


49

241. Université Catholique de Louvain, “Resistance to β-Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, Brussels, Belgium, September 2008.

242. Harvard University, "Resistance to β-Lactam Antibiotics in Methicillin-

Resistant Staphylococcus aureus (MRSA)", Boston, September 2008. 243. University of Rosario, "Resistance to β-Lactam Antibiotics in Methicillin-

Resistant Staphylococcus aureus (MRSA)", Rosario, Argentina, November, 2008. 244. University of Missouri-Columbia School of Medicine, "Role of the Active Site Zinc Ion of

Matrix Metalloproteinases in Enzyme Activation and Its Subversion in the Process of Selective Inhibition", Columbia, December 2008.

245. Indiana University School of Medicine—Northwest, "Bacterial Cell Wall", December

2008. 246. Plenary Lecture, The Ninth Winter Conference on Bioorganic & Medicinal Chemistry

“Resistance to β-Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, Steamboat, Colorado, January 2009.

247. University of Georgia, “Resistance to β-Lactam Antibiotics in Methicillin-Resistant

Staphylococcus aureus (MRSA)”, Athens, March 2009. 248. Workshop on Biomedical Research, “Bacterial Cell Wall”, University of Notre Dame,

March 2009. 249. New York University, “Bacterial Cell Wall”, April 2009 250. The National Meeting of the American Society for Microbiology, “Bacterial Cell Wall”,

Philadelphia, May 2009. 251. Gordon Conferences on Matrix Metalloproteinases, “Progression of Studies on

Mechanism-based Inhibitors for Gelatinases”, Diablerets, Switzerland, August 2009. 252. Distinguished Lecture Series, Academia Sinica, “Bacterial Cell Wall”, Taipei, Taiwan,

September 2009. 253. Distinguished Lecture Series, Academia Sinica, “Resistance to β-Lactam Antibiotics in

Methicillin-Resistant Staphylococcus aureus (MRSA)”, Taipei, Taiwan, September 2009. 254. AstraZeneca, “Bacterial Cell Wall”, Waltham, MA, September 2009. 255. The J. Clarence Karcher Lecture, University of Oklahoma, “Bacterial Cell Wall”, Norman,

OK, October 2009. 256. The Meeting of the UK-Canada Bacterial Cell Wall Biosynthesis Network, “Turnover of

the Bacterial Cell Wall”, Warwick, The United Kingdom, November 2009. 257. Texas Tech University, “Bacterial Cell Wall”, Lubbock, Texas, November 2009. 258. Texas Tech University, “Resistance to β-Lactam Antibiotics in Methicillin-Resistant

Staphylococcus aureus (MRSA)”, Lubbock, Texas, November 2009.


50

259. Consejo Superior de Investigaciónes Científicas (CSIC), “Resistance to β-Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, Madrid, Spain, December 2009.

260. University of Toledo, “Bacterial Cell Wall”, Toledo, Ohio, March 2010. 261. Gordon Research Conference on New Antibacterial Drug Discovery and Development,

“The BlaR Protein and Its Involvement in Methicillin-Resistance in Staphylococcus aureus”, Galveston, TX, March 2010.

262. Indiana University School of Medicine, Department of Biochemistry, “Resistance to β-

Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, Indianapolis, Indiana, April 2010.

263. Purdue University, “Bacterial Cell Wall”, West Lafayette, Indiana, April 2010. 264. Frontiers in Biomedical Research, “Mechanism of Matrix Metalloproteinase Activation and

the Process of Selective Inhibition”, Fargo, May 2010. 265. The 110th General Meeting of the American Society for Microbiology, “Cell Wall

Turnover”, San Diego, May 2010. 266. The Second Sigma-Aldrich Symposium, “Pared Celular Bacteriana”, Unidad Zacatenco,

Mexico, April 2010. 267. Gordon Research Conference on Bioorganic Chemistry, “Bacterial Cell Wall Turnover”,

Andover, New Hampshire, June 2010. 268. World Congress of Pharmacy & Pharmaceutical Sciences 2010, 70th International Congress

of Pharmaceutical Federation, “Resistance to β-Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA)”, Lisbon, Portugal, August 2010.

269. Cubist Pharmaceuticals, “Bacterial Cell Wall”, Boston, October 2011. 270. The Inaugural Indiana Medicinal Chemistry Symposium, “Resistance to β-Lactam

Antibiotics in Methicillin-Resistance in Staphylococcus aureus”, Indianapolis, October 2010.

271. University of Kansas, “Bacterial Cell Wall”, November 2010. 272. Brigham Young University, “Resistance to β-Lactam Antibiotics in Methicillin-Resistant

Staphylococcus aureus (MRSA)”, Provo, January 2011. 273. El Colegio Nacional (counterpart to the US National Academy of Sciences), “Elucidation

of Mechanisms of Diseases of Matrix and Their Pharmaceutical Intervention”, Mexico City, Mexico, February 2011.

274. Molecular Biosciences Lecture, Wichita State University, “Resistance to β-Lactam

Antibiotics in Methicillin-Resistance Staphylococcus aureus”, Wichita, March 2011. 275. York University, “Bacterial Cell Wall”, Toronto, Canada, April 2011. 276. Distinguished Lecture, Florida International University, “Bacterial Cell Wall”, Miami,

April 2011.


51

277. The Cold Spring Harbor Laboratory: Antibiotic Resistance: Past, Present, Future, New

York, May 2011. 278. The 94th Canadian Chemistry Conference, “Resistance to β-Lactam Antibiotics in

Methicillin-Resistance Staphylococcus aureus”, Montreal, Canada, June 2011. 279. Gordon Research Conference on Matrix Metalloproteinases, “Stopping and Smelling the

Roses: Tools in Elucidation of the Details of MMP-Dependent Diseases”, Rhode Island, August, 2011.

280. University of Missouri, Pathology Grand Rounds/Translational Biomedicine Seminar

Series, “From Mechanistic Understanding to Medicinal Intervention: Diabetic Wound Healing and Methicillin-Resistant Staphylococcus aureus”, Columbia, October 2012.

281. University of South Florida, “Bacterial Cell Wall”, Tampa, December 2011. 282. Frontiers in Drug Discovery Lecture, Medical University of South Carolina,

”Pharmacological Protection of Neurons Subsequent to Stroke and Traumatic Brain Injury”, Charleston, March 2012.

283. The 243rd ACS National Meeting, Early Events in Recycling of Bacterial Cell Wall, San

Diego, March 2012. 284. The 243rd ACS National Meeting, β-Lactam Antibiotic-Resistance Machineries in Gram-

Negative and Gram-Positive Bacteria, San Diego, March 2012. 285. The 243rd ACS National Meeting, Mechanism of Resistance to β-Lactam Antibiotics in

Methicillin-Resistant Staphylococcus aureus (MRSA), San Diego, March 2012. 286. Second International Helmholtz-Institute for Pharmaceutical Symposium, Mechanism of

Resistance to β-Lactam Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA). Saarbrücken, Germany, June 2012.

287. University of Sienna, School of Medicine, How Staphylococcus aureus Became

Methicillin-Resistant Staphylococcus aureus (MRSA), July 2012. 288. Global Health Colloquium, University of Notre Dame, How Staphylococcus aureus

Became Methicillin-Resistant Staphylococcus aureus (MRSA), September 2012. 289. Cubist Pharmaceutical Co., How Staphylococcus aureus became Methicillin-Resistant

Staphylococcus aureus (MRSA), September 2012. 290. The 6th Brazilian Symposium on Medicinal Chemistry, Medicinal Chemistry for Diseases

of Matrix, Canela, Rio Grande do Sul, Brazil, October 2012. 291. Office of Naval Research, Washington, D.C., Traumatic Brain Injury, November 2012. 292. Universidade Federal do Rio Grande do Sul, How Staphylococcus aureus Became

Methicillin-Resistant Staphylococcus aureus (MRSA), Bacterial Cell Wall, Brazil, November 2012.

293. University of Maryland, How Staphylococcus aureus Became Methicillin-Resistant

Staphylococcus aureus (MRSA), February 2013.


52

294. University of Maryland, Baltimore County, How Staphylococcus aureus Became

Methicillin-Resistant Staphylococcus aureus (MRSA), January 2013. 295. University of Notre Dame, Interdisciplinary Science Seminar, Intervention of Diseases of

Extracellular Matrix, March 2013. 296. The Smissman Award Symposium Honoring Richard Silverman, Therapeutic Intervention

in Neurological Diseases of Matrix, ACS Spring Meeting, New Orleans, April 2013. 297. The 5th Chicago Organic Symposium, Organic Chemistry and Elucidation of Complex

Biological Systems, June 2013. 298. Baxter Pharmaceutical Company, Bacterial Cell Wall, Its Synthesis, Recycling and Link to

Antibiotic Resistance, July 2013. 299. The United States National Academy of Sciences, The Complex Resistance Machineries

for β-Lactam Antibiotics in Gram-Negative and Gram-Positive Bacteria, Washington, DC, September 2013.

300. Congreso Argentino de Microbiologia, How Staphylococcus aureus Became Methicillin-

Resistant Staphylococcus aureus (MRSA), Buenos Aires, September 2013. 301. University of Rosario, Cell-Wall Recycling and Links to Virulence and Antibiotic

Resistance in Gram-Negative Bacteria, Rosario, Argentina, September 2013. 302. The Watanabe Lecture, The Fifth August M. Watanabe Symposium in Biotechnology,

How Staphylococcus aureus Became Methicillin-Resistant Staphylococcus aureus (MRSA), Indiana University, October 2013.

303. Florida International University, How Staphylococcus aureus Became Methicillin-

Resistant Staphylococcus aureus (MRSA), Indiana University, October 2013. 304. International Union of Biochemistry and Molecular Biology Conference on Host-Microbe

Interactions, How Staphylococcus aures became Methicillin-Resistant Staphylococcus aures (MRSA), Marrakesh, Morocco, November 2013.

305. Annual Meeting of the American Association of Pharmaceutical Scientists (AAPS),

Pharmacological Protection of Neurons Subsequent to Stroke and Traumatic Brain Injury, San Antonio, November 2013.

306. The Eck Institute Retreat, The University of Notre Dame, Cell-Wall Recycling and Links

to Virulence and Antibiotic Resistance in Gram-Negative Bacteria, January 2014. 307. Merck & Co., "How Staphylococcus aureus Became Methicillin-Resistant Staphylococcus

aureus (MRSA)", Kenilworth, NJ, February 2014. 308. Department of Pharmacology, Case Western Reserve University, How Staphylococcus

aureus Became Methicillin-Resistant Staphylococcus aureus (MRSA), Cleveland, April 2014.

309. Society for General Microbiology, Annual Meeting, Early Events in Recycling of Cell

Wall, Liverpool, UK, April 2014.


53

310. Universidade Federal do Rio Grande do Sul, Cell-Wall Recycling and Links to Virulence and Antibiotic Resistance in Gram-Negative Bacteria, Porto Alegre, Brazil, April 2014.

311. Universidade Federal do Rio Grande do Sul, Power of Biomedical

Interdisciplinary/Multidisciplinary Research, Porto Alegre, Brazil, April 2014. 312. The 12th β-Lactamase Conference, Allostery in the Function of Penicillin-Binding 2a of

Methicillin-Resistant Staphylococcus aureus (MRSA), Gran Canaria, Spain, June 2014. 313. Universidad de La Laguna, Descubrimiento del Sitio Alostérico en PBP2a, Santa Cruz de

Tenerife, Islas Canarias, Spain, June 2014. 314. The Nankai University, Power of Biomedical Interdisciplinary/Multidisciplinary Research

Applied to Discovery of Antibiotics, Tianjin, China, July 2014. 315. The Nankai University, Organic Chemistry and Elucidation of Complex Biological

Systems, Tianjin, China, July 2014. 316. Universidade de São Paulo, Instituto de Química, Organic Chemistry and the Elucidation

of Complex Biological Systems, São Paulo, Brazil, August 2014. 317. Universidade Estadual de Campinas, Organic Chemistry and the Elucidation of Complex

Biological Systems, Campinas, Brazil, August 2014. 318. Universidade Federal de Rio de Janeiro, Organic Chemistry and the Elucidation of

Complex Biological Systems, Campinas, Brazil, August 2014.

319. Eli Lilly Grand Rounds Lecture, How Staphylococcus aureus Became Methicillin-Resistant Staphylococcus aureus (MRSA), Indianapolis, August 2014.

320. Palacky University of Olomouc, Allostery in Catalysis by Penicillin-Binding Protein 2a of

Methicillin-Resistant Staphylococcus aureus (MRSA), Antibiotic Resistance and Discovery of New Antibiotics, Olomouc, Czech Republic September 2014.

321. Miami University, Department of Chemistry, Power of Biomedical

Interdisciplinary/Multidisciplinary Research Applied to Discovery of Antibiotics October 2014.

322. The Scott Medal Symposium in honor of John Blanchard, Cell-Wall Recycling and

Signaling in Bacteria, Texas A & M University, October 2014. 323. Leloire Institute, Cell Wall as Target for Discovery of Novel Antibiotics, Buenos Aires,

Argentina, May 2015. 324. University of Rosario, Bacterial Cell Wall, Synthesis of Its Components and Its

Biochemistry, Rosario, Argentina, May 2015.

325. Universidad de Montevideo, “Cell Wall as Target for Antibiotics”, Montevideo, Uruguay, May 2015.

326. Joint Great Lakes/Central Regional ACS Meeting, Allostery in Catalysis by Penicillin-

Binding Protein 2a of Methicillin-Resistant Staphylococcus aureus (MRSA), Grand Rapids, May 2015.


54

327. Ohio State University, Cell Wall as Target for Discovery of Novel Antibiotics, Columbus, Ohio, June 2015.

328. The 98th National Meeting of the Canadian Society for Chemistry, Cell Wall as Target for

Antibiotics, Ottawa, Canada, June 2015. 329. Universidad de la República, Cell Wall as Target for Antibiotics, Montevideo, Uruguay,

August 2015. 330. The Great Wall Symposium, Cell Wall as Target for Discovery of Novel Antibiotics,

Florence, Italy, September 2015. 331. The 9th General Meeting of the International Proteolysis Society, CellWall Proteolysis in

Signalling in Pseudomonas aeruginosa, a Nexus for the Induction of Antibiotic Resistance, Penang, Malaysia, October 2015.

332. Nankai University, Antibiotic Resistance in Methicillin-Resistant Staphylococcus aureus

and Involvement of Allostery in the Function of Penicillin-Binding Protein 2a, Tianjin, China, October 2015.

333. Faculty of Chemistry, Pontificia Universitad Católica de Chile, Cell Wall as Target for

Discovery of Novel Antibiotics, November 2015, Santiago de Chile. 334. Department of Biochemistry, Pontificia Universitad Católica de Chile, Pharmacological

Protection of Neurons Subsequent to Stroke and Traumatic Brain Injury, November 2015, Santiago de Chile.

335. School of Medicine, Pontificia Universitad Católica de Chile, How Staphylococcus aureus

Became Methicillin-Resistant Staphylococcus aureus (MRSA), November 2015, Santiago de Chile.

336. University of Alberta, Cell Wall as Target for Antibiotics, Alberta, Canada, November

2015. 337. The International Chemical Congress of Pacific Basin Societies (“Pacific Chem”), Cell

Wall as Target for Discovery of Novel Antibiotics, Honolulu, December 2015. 338. Northwestern University School of Medicine, Cell-Wall Recycling and Signaling in

Bacteria, January 2016, Chicago. 339. American Society for Biochemistry and Molecular Biology (ASBMB), the 2016 Annual

Meeting, New Antibiotics for the Post-Antibiotic Era, April 2016, San Diego. 340. Purdue University, Department of Medicinal Chemistry, Resistance to β-Lactam

Antibiotics in Methicillin-Resistant Staphylococcus aureus (MRSA) and Its Subversion in Discovery of Novel Antibiotics, April 2016, West Lafayette.

341. North Carolina State University, Resistance to β-Lactam Antibiotics in Methicillin-

Resistant Staphylococcus aureus (MRSA) and Its Subversion in Discovery of Novel Antibiotics, April 2016, Raleigh.

342. Universidad de Rioja, Discovery of the Allosteric Site in PBP2a, May 2016, Logroño,

Spain.


55

343. Dovetailing of Experiment and Computation in Biomedical Sciences, The Second Heidelberg-Notre Dame Summer School in Computational Chemistry, Notre Dame, July 2016.

344. The Joint Symposium in Chemical Sciences University of Notre Dame/Pontificia

Universidad Católica, New Antibiotics for the Post-Antibiotic Era, Santiago de Chile, September 2016.

345. National Meeting of the German Pharmaceutical Society (DPhG), New Antibiotics for the

Post-Antibiotic Era, October 2016, Munich, Germany. 346. University of Heidelberg, Research at the Interface of Chemistry and Biology: Discovery

of Novel Antibacterial Agents, Heidelberg, Germany, October 2016. 347. Keynote Speaker, The 12th Midwest Carbohydrate and Glycobiology Symposium (MCGS),

Muropeptides and Signaling in Gram-Negative Bacteria, Mount Pleasant, October 2016. 348. The 26th Keck Annual Research Conference, New Antibiotics for the Post-Antibiotic Era,

October 2016, Houston. 349. Fundación MEDINA, Resistance to β-Lactam Antibiotics in Methicillin-Resistant

Staphylococcus aureus (MRSA) and Its Subversion in Discovery of Novel Antibiotics, November 2016, Granada, Spain.

350. The 25th Enzyme Mechanisms Conference, Nexus Among Cell-Wall Turnover, Antibiotic

Resistance and Virulence in Pseudomonas aeruginosa, January 2017, St. Petersburg, Florida.

351. The 13th Beta-Lactamase Meeting, Nexus between Cell-Wall Turnover and β-Lactam

Antibiotic Resistance, June, 2017, Santo Stefano di Sessanio, Italy. 352. Universidad Nacional Autónoma de México (UNAM), Nexus Among Cell-Wall Turnover,

Antibiotic Resistance and Virulence in Pseudomonas aeruginosa, October 2017, Mexico City, Mexico.

353. Instituto Politécnico Nacional, Centro de Investigación y Estudios Avanzados

(CINVESTAV), Nexus Among Cell-Wall Turnover, Antibiotic Resistance and Virulence in Pseudomonas aeruginosa, October 2017, Mexico City, Mexico.

354. Annual Meeting of the American Society of Pharmacognosy (ASP), **, July 2018,

Lexington, KY. 355. New Antibacterial Discovery & Development Gordon Research Conference, Non-Natural-

Product Antibiotics and Resistance Potentiators, March 2018, Ventura, California. 356. Case Western University, Complex Biological Machineries: Bacterial Cell Wall, Its

Turnover and Link to Antibiotic Resistance, April 2018 357. International Conference on Pseudomonas, Nexus Among Cell-Wall Turnover, Antibiotic

Resistance and Virulence in Pseudomonas aeruginosa, July 2019, Malaysia.

Lectures to General Audience:


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1. Devine-Child High School, Southfield, MI, "Antibiotics: The Twentieth-Century "Silver Bullets" and How They Are Being Tarnished", January 1998.

2. Universidad de Murcia, Murcia, Spain, “Antibioticos: Pasado, Presente, y Futuro”, April

2001.

3. University of Hong Kong, Hong Kong, China, "Antibiotics: The Twentieth-Century "Silver Bullets" and How They Are Being Tarnished", May 2006.

4. The Merck Frosst Lecture, Simon Fraser University, Vancouver, Canada, "Antibiotics:

The Twentieth-Century "Silver Bullets" and How They Are Being Tarnished", March 2007.

5. Reunion Weekend Lecture, University of Notre Dame, "Antibiotics: The Twentieth-

Century "Silver Bullets" and How They Are Being Tarnished", June 2009.

6. Windmoor Lecture Series, University of Notre Dame, "Antibiotics: The Twentieth-Century "Silver Bullets" and How They Are Being Tarnished", March 2012.

7. Hesburgh Lecture, Notre Dame Club of Ventura County, California, "Antibiotics: The

Twentieth-Century "Silver Bullets" and How They Are Being Tarnished", March 2014.

Curriculum Vitae List of Publications and Research Funding ...

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